ID A0A3A9UPG0_9FLAO Unreviewed; 911 AA.
AC A0A3A9UPG0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:AXT21173.1};
GN ORFNames=D1817_15275 {ECO:0000313|EMBL:AXT21173.1};
OS Flavobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT21173.1, ECO:0000313|Proteomes:UP000260281};
RN [1] {ECO:0000313|EMBL:AXT21173.1, ECO:0000313|Proteomes:UP000260281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU392 {ECO:0000313|EMBL:AXT21173.1,
RC ECO:0000313|Proteomes:UP000260281};
RA Song W., Thomas T., Edwards R.;
RT "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT using PacBio sequencing.";
RL Submitted (AUG-2018) 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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP031964; AXT21173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9UPG0; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000260281; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
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; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 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; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 Reference proteome {ECO:0000313|Proteomes:UP000260281}.
FT DOMAIN 87..126
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 148..167
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 191..220
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 227..283
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 911 AA; 100843 MW; EE0C4B70151C6559 CRC64;
MERLKVAYID NQAFEIVEGE TMLAFIKRYK EKNLVPTLCD APNLDPFGSC RVCSVEVALE
KNGPLKTMAS CHSPVAEGQY IYTSSEAIKA LRKNIIELVL TDHPLDCLTC EVNGNCELQT
VAAQVGIREV RYPEGDNHLY RLKDLSHPYM TSDLSKCINC YRCVRACDEV QGEFVLSMSG
RGFDSHIIKG FDESFMESDC VSCGACSQAC PTSAISDVFQ SKAIAATDTT RTICTYCGVG
CNLEVSTTNG EILSIQAPYD AEVNQGHTCI KGRYAFKFYN HQDRLDSPMI KRNGEFEKVT
WNEVYDYIAT KLNGYKTEFG PDFIAGISSA RCTNEENYLM QKFIRTVIGT NNIDGCARVC
HSPTALGMQR AYGTGAATNS IDDLKDANCI MVIGANPTDA HPVTGAKLKQ FAMKSDNISI
VIDPRRTELA KYATHHIALR PGTNVAVLNM MMYYIISEGL ADSKFIESRT EGFDAFKAEI
LNIDLDASEA IIGVDRNEIK AAAIAYATAS NAMSFHGLGV TEHSQGTFTV IQIADLALLT
GNIGRRGVGV NPLRGQNNVQ GSADMGVQPH QGAGYLDVTN AAVNEKYNAF YGVDVPKHIG
YKIPEMFDAA LDGKLKAIWI IGEDIVQTDP NTQKVIKALE STDLVIVQEL FMTETAKYAD
VILPGASFLE KSGTFTNGER RVQAVRQVVK PIEGSKPDGQ IIVEIMNRMG YPQPDYTPDG
MLEEISQIVP FFEGITWDRL GKNGLQWPVA KDGTDTQILH QTDFKRGKGY FEFNAWRETE
EINEHGKTFP YILTTNRELE HYNCGAMTRR TANEEILQDD YLMVNPEDAA QNLINDGDYV
CLESPRGKVD VKARITDEVK PGVLSTTFHF PEIMINNLTG DIHDSEAMCP EYKVVAVRIR
KSKGKFKEVL S
//
