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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
DOI=10.1271/bbb.66.489; PubMed=12005040 [NCBI, ExPASy, EBI, Israel, Japan]
Sahara T.,
Takada Y.,
Takeuchi Y.,
Yamaoka N.,
Fukunaga N.;
"Cloning, sequencing, and expression of a gene encoding the monomeric isocitrate dehydrogenase of the nitrogen-fixing bacterium, Azotobacter vinelandii.";
Biosci. Biotechnol. Biochem. 66:489-500(2002).
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[2]
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PRELIMINARY PROTEIN SEQUENCE OF 229-251 AND 255-260.
DOI=10.1021/bi00701a007; PubMed=4149369 [NCBI, ExPASy, EBI, Israel, Japan]
Edwards D.J.,
Heinrikson R.L.,
Chung A.E.;
"Triphosphopyridine nucleotide specific isocitrate dehydrogenase from Azotobacter vinelandii. Alkylation of a specific methionine residue and amino acid sequence of the peptide containing this residue.";
Biochemistry 13:677-683(1974).
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[3]
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X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF COMPLEXES WITH ISOCITRATE; MANGANESE AND NADP, AND SUBUNIT.
DOI=10.1016/S0969-2126(02)00904-8; PubMed=12467571 [NCBI, ExPASy, EBI, Israel, Japan]
Yasutake Y.,
Watanabe S.,
Yao M.,
Takada Y.,
Fukunaga N.,
Tanaka I.;
"Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication.";
Structure 10:1637-1648(2002).
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- CATALYTIC ACTIVITY: Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.
- CATALYTIC ACTIVITY: Oxalosuccinate + NADP+ = 2-oxoglutarate + CO2 + NADPH.
- COFACTOR: Binds 1 magnesium or manganese ion per subunit.
- ENZYME REGULATION: Inhibition of this enzyme by phosphorylation regulates the branch point between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth. The phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (aceK).
- BIOPHYSICOCHEMICAL PROPERTIES:
- SUBUNIT: Monomer.
- SUBCELLULAR LOCATION: Cytoplasm.
- DOMAIN: This molecule consists of two distinct domains, a small domain and a large domain. The structure of the large domain repeats a motif observed in the dimeric IDH. Such a fusional structure by domain duplication enables a single polypeptide chain to form a structure at the catalytic site that is homologous to the dimeric IDH, the catalytic site of which is located at the interface of two identical subunits.
- SIMILARITY: Belongs to the monomeric-type IDH family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 741 AA [This is the length of the unprocessed precursor] |
Molecular weight: 80390 Da [This is the MW of the unprocessed precursor] |
CRC64: 29FF35278E5AED8B [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSTPKIIYTL TDEAPALATY SLLPIIKAFT GSSGIAVETR DISLAGRLIA TFPEYLTDTQ
70 80 90 100 110 120
KISDDLAELG KLATTPDANI IKLPNISASV PQLKAAIKEL QQQGYKLPDY PEEPKTDTEK
130 140 150 160 170 180
DVKARYDKIK GSAVNPVLRE GNSDRRAPLS VKNYARKHPH KMGAWSADSK SHVAHMDNGD
190 200 210 220 230 240
FYGSEKAALI GAPGSVKIEL IAKDGSSTVL KAKTSVQAGE IIDSSVMSKN ALRNFIAAEI
250 260 270 280 290 300
EDAKKQGVLL SVHLKATMMK VSDPIMFGQI VSEFYKDALT KHAEVLKQIG FDVNNGIGDL
310 320 330 340 350 360
YARIKTLPEA KQKEIEADIQ AVYAQRPQLA MVNSDKGITN LHVPSDVIVD ASMPAMIRDS
370 380 390 400 410 420
GKMWGPDGKL HDTKAVIPDR CYAGVYQVVI EDCKQHGAFD PTTMGSVPNV GLMAQKAEEY
430 440 450 460 470 480
GSHDKTFQIP ADGVVRVTDE SGKLLLEQSV EAGDIWRMCQ AKDAPIQDWV KLAVNRARAT
490 500 510 520 530 540
NTPAVFWLDP ARAHDAQVIA KVERYLKDYD TSGLDIRILS PVEATRFSLA RIREGKDTIS
550 560 570 580 590 600
VTGNVLRDYL TDLFPIMELG TSAKMLSIVP LMSGGGLFET GAGGSAPKHV QQFLEEGYLR
610 620 630 640 650 660
WDSLGEFLAL AASLEHLGNA YKNPKALVLA STLDQATGKI LDNNKSPARK VGEIDNRGSH
670 680 690 700 710 720
FYLALYWAQA LAAQTEDKEL QAQFTGIAKA LTDNETKIVG ELAAAQGKPV DIAGYYHPNT
730 740
DLTSKAIRPS ATFNAALAPL A
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P16100 in FASTA format |
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