ID A0A0J1GJR0_9GAMM Unreviewed; 1395 AA.
AC A0A0J1GJR0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KLU99919.1};
GN ORFNames=ABT58_15820 {ECO:0000313|EMBL:KLU99919.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99919.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLU99919.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99919.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU99919.1}.
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DR EMBL; LDOV01000027; KLU99919.1; -; Genomic_DNA.
DR RefSeq; WP_047875377.1; NZ_PYMF01000023.1.
DR PATRIC; fig|754436.4.peg.3354; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000036426; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
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; cd02790; MopB_CT_Formate-Dh_H; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
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; IPR041925; CT_Formate-Dh_H.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; SSF54292; 2Fe-2S ferredoxin-like; 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; PS00551; MOLYBDOPTERIN_PROK_1; 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 Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000036426}.
FT DOMAIN 1..77
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 611..640
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 662..690
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 699..757
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1395 AA; 152433 MW; D7C95F098A33D98C CRC64;
MNNVIIDGQS IAVDGQQSLL DVANAHQIEI PSLCGLNKSG EKVPCDLCMV EIDGQGMQRA
CEVTAQAGMS VTTQSDALSA HRRQALNRIM ADHYADCEAP CQTACPAGVD IQSYLYHIAQ
NDHQKAVEVI KRTLPMPLSI GRVCPAFCEA ECRRGIVDEP LAIRQLKRHA ADIDLEAQEQ
YVPPRKADKG KRVAIIGSGP GGLSCGYYLS NEGYAVTVFE SMPKAGGWLR YGIPEYRLPK
AILDKEIELI CRNGMEVKTN QSLGKDMQLS ELVADYDAVC LAVGASQAVE MHYTGSDLDG
CYLGVDYLKD YVTDKQYTTG KKVAVIGGGN TAIDCARTAV RDGADTTLIY RRTRDEMPAE
DYEIAEAEHE GVKFHFLTNP VENMADENGR VTDVKLEKMA LGEPDASGRR SPVPTGEYVV
EHFDTVISAV SQKPDLSFLN DDTLELPITR WQTVESCEHT MHVGVENIFS IGDLRRGPAT
AIEAVADGRV AAHAIDRYLH GDMAAVPVKP FNAQKAASVK QVDPAQFAGI QKAMRAIMPE
LTTAERELSF AEVETGFDNE DAMREAARCL ECGCQANTDC KLRDYSTEYK AEQNAEAMAD
CQKFAVDNSA EFIVFDANRC ISCGQCVQTC NEKTVHGVLS FMKNEDGTSA NRPECRPGFD
NRQPMGDSNC VQCGACVQVC PTGALVDGRD RSQGRIEMLT PVDTICTYCG VGCKVTMFVD
EATNKIRYVQ GAKSSPVNQG MLCVKGRFGF DFIQSEERLT HPLIRRGGRN GKLEKATWSE
AIALVADKLG EIKATHGGNA LAGFSSAKTT NEDNFAFQKF FRRELLTNNI DHCARLCHST
TVTGLEASLG SGAMTNDIPS IQHSDLIFII GSDTTAAHPI IASHIKQALR AGKARLVVAD
PKHVEIADHA SLYVAHRPGT DVMLLNGIMQ QIIKNGWQDE AYIAERVTGF DVLKDEVMRE
DYSPANVELI TGVKQADLLH MAEMIGTAER TAVYYSMGIT QHTTGHDNVR SIANLQMLCG
NIGIEGGGIN PLRGQSNVQG ACDMGALPKD FPGYQKIRNP EAHQKFAKAW DCPELPAEDG
LTLTEIVDAA CQQQVRGLYV MGENPVLSDP DQKHVLEALA TLDFLVVQDI FLTETAQLAD
VVLPSFSFAE KSGHFTNTER RVQRVSPALR APGEAMEDWR IIQTIANAMG SDWAYESVRD
ITDEINVLTP QYAGITWDRV GAEGIQWPCP STEHAGTRIM HKDSMMRGKG EMAAVPFRYA
AELPDPEYPM VLTTGRLLEQ FHTGTMTRKT KGLDNLAGPR AMISVQDAER LGISNGEMLK
VSTRRGSIET PAFVTKRMQE GVIFVPFHFV ESAANKLTVT ATDPHAKIPE FKVAAVKIEK
AHVAETEAEA EILPA
//