[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00279380; PubMed=1465107 [NCBI, ExPASy, EBI, Israel, Japan] Saleeba J.A., Cobbett C.S., Hynes M.J.; "Characterization of the amdA-regulated aciA gene of Aspergillus nidulans."; Mol. Gen. Genet. 235:349-358(1992).

Comments

CATALYTIC ACTIVITY: Formate + NAD⁺ = CO₂ + NADH.
SUBUNIT: Homodimer (By similarity).
INDUCTION: Acetate induction mediated by amda regulatory gene.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z11612; CAA77687.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S30088; S30088.

3D structure databases

HSSP

P33160; 2NAC. [HSSP ENTRY / PDB]

ModBase

Q03134.

Ontologies

GO:0008863;	Molecular function: formate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0016616;	Molecular function: oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.

ProtoNet

Q03134.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 377`	`377`	`Probable formate dehydrogenase.`	`PRO_0000076024`
`ACT_SITE`	`271 271`		`By similarity.`
`ACT_SITE`	`324 324`		`Proton donor (By similarity).`

Sequence information

Length: 377 AA [This is the length of the unprocessed precursor]

Molecular weight: 41531 Da [This is the MW of the unprocessed precursor]

CRC64: 5219F5FEBCC931CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLYDGGSHA KDQPGLLGTT ENELGIRKWI EEQGHTLVTT SDKDGENSTF DKELVDAEVI 

        70         80         90        100        110        120 
ITTPFHPGYL TAERLAKAKN LKLAVTAGIG SDHVDLDAAN KTNGGITVAE VTGSNVVSVA 

       130        140        150        160        170        180 
EHVVMTILLL VRNFVPAHDQ IRNGDWNVAA VAKNEFDLEN KVVGTVGVGR IGERVLRRLK 

       190        200        210        220        230        240 
PFDCKELLYY DYQPLRPEVE KEIGARRVDS LEEMVSQCDV VTINCPLHEK TRGLFNKELI 

       250        260        270        280        290        300 
SKMKPGKSAL LYLIIPMLMY HKGSWLVNTA RGAIVVKEDV AEALKSGHLR GYGGDVWFPQ 

       310        320        330        340        350        360 
PAPKEHPLRY AEHPWGGGNA TVPHMSGTSL AAQIRYANGT KAILDSYFSG RFDYQPQDLI 

       370 
VHGGDYATKA YGQREKK

Q03134 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools