ID G0AZM3_9GAMM Unreviewed; 1425 AA.
AC G0AZM3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=Sbal175_3399 {ECO:0000313|EMBL:AEG12633.1};
OS Shewanella baltica BA175.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG12633.1, ECO:0000313|Proteomes:UP000002249};
RN [1] {ECO:0000313|EMBL:AEG12633.1, ECO:0000313|Proteomes:UP000002249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA175 {ECO:0000313|EMBL:AEG12633.1,
RC ECO:0000313|Proteomes:UP000002249};
RX PubMed=22328742; DOI=10.1128/JB.06468-11;
RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA Konstantinidis K.T.;
RT "Genome sequencing of five Shewanella baltica strains recovered from the
RT oxic-anoxic interface of the Baltic Sea.";
RL J. Bacteriol. 194:1236-1236(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002767; AEG12633.1; -; Genomic_DNA.
DR RefSeq; WP_006080386.1; NC_017571.1.
DR KEGG; sbb:Sbal175_3399; -.
DR HOGENOM; CLU_000422_0_1_6; -.
DR Proteomes; UP000002249; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43742:SF2; ASSIMILATORY NITRATE REDUCTASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:AEG12633.1}.
FT DOMAIN 1..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 642..661
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 697..727
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 735..793
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1425 AA; 154510 MW; 5DE5EF82248AC565 CRC64;
MIELRIDDQV LSVNSTDNLL QAAHAAGIAI PSLCDPSAAS QQLGTHAHTH VQADKQACNL
CVVQIENADA SLRCVRACET LVAAGMRVIT QSEWLSQQRK QALTAILSDH FADCEAPCQQ
ACPAGVDVQS YLYHIAQGNH TEAVKVIKQT LPLPLSIGRV CPAFCEAQCR RGLVDEPIAI
RQLKRHAADL DLADGEKGGT SYVPPRQADT GKKVAIIGAG PAGLSAGYYL SNQGHSVEIF
EAMPQAGGWL RYGIPEYRLP KAILDKEIAL LCHNGLTIHT ETCLGHEVHL NQLVEDFDAV
CLAIGAQKAV PMDYPGSTLK GCYLGVDYLK DHCLEKTLVL GKKVAVIGGG NTAIDCARTA
VREGCDVTLI YRRTRAEMPA EAYEVHEAEV EGVKFHFLTN PLENHSDAQG RVHAVTFAKM
ALGEADASGR RAPVDTGETF TQDFDTVIAA VSQTPDLSFM QDPASPLSQG TLALSRWNTF
IGCEHTMSSG VEKLFVVGDA RRGPATAVAA IGDGHKAAIA IDKLLKQGLS CELHANAFNS
AKAISKAVTQ DLPATDFYPA VPRKARLTMP ELSAVQRLLN YGEVELGFAP DAAMQEAARC
LECACQANTD CKLRDYATDY HVEPKSLNTQ SARKFSVDKS SPFIQFDANR CISCGKCVDV
CQLQSGHCAI QFAHDSYQAL PQDLSETIER RAPRVGFSAS MADSKCVQCG NCVQVCPTGA
LVDARDKRQG DETPLKTAST ICTYCGVGCR LDLKIDASTN QIRHIEGNKE SVVNQGMLCV
KGRFGFDFIH SEKRLTTPLI RKNGQLTPST WPEAIAYVAE HLQQIKQQYG SNALASLASA
KATNEENFLL QKFVRSILGT NNIDHCARLC HSSTVTGLQQ SIGSGAMTND IPSIQASDVI
FIIGSDTSSA HPIIASKIKQ AVALHGAKLM VADPKRVAIA DSAQLYVAHR PGTDVMLLNA
IMAEIIRNNW QDKSYIVART EGVNALYAEL AKADYSLKNA ALITGVTAED IACIARTIGT
AEKTAIYYAM GITQHTTGHD NVTAISNLQL LCGNIGVEGA GINPLRGQSN VQGACDMGAL
PNFFSGYQKV TDIHARMRFE AHWQTPLSAE IGVTATHMMH DISKGYIKAL YVMGENPVLS
DPDQAHVLRA LNAIDFLVVQ DIFLTETAEL ADVVLPAAAF VEKRGHFTNT ERRVQRLEQA
LLPPGEALPD WQIVQAIANA MGAAWDYPNE EAIWQEINEL TPQYRGITWQ RLSTRDDGKI
PQGIQWPCPD ETHPGTPIMH QGQFTRGLGK FTPVSYRLPA EMPCSEYPLT LSTGRLLEQF
HTGTLTRKTA GLDLLGSPKV MISVYDAEQL GIGNGDKIKL TTRRGEIEID AFVTKRAQAG
VLFLPFHFVE AAANKLTINA LDPVAFIPEY KVCSVRVEWV AEKIN
//
