ID S3IIX1_9ENTR Unreviewed; 716 AA.
AC S3IIX1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EPF13020.1};
GN ORFNames=HMPREF0201_04623 {ECO:0000313|EMBL:EPF13020.1};
OS Cedecea davisae DSM 4568.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cedecea.
OX NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF13020.1, ECO:0000313|Proteomes:UP000014585};
RN [1] {ECO:0000313|EMBL:EPF13020.1, ECO:0000313|Proteomes:UP000014585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF13020.1,
RC ECO:0000313|Proteomes:UP000014585};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2013) 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 -!- 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:EPF13020.1}.
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DR EMBL; ATDT01000038; EPF13020.1; -; Genomic_DNA.
DR RefSeq; WP_016538790.1; NZ_KE161030.1.
DR AlphaFoldDB; S3IIX1; -.
DR STRING; 566551.HMPREF0201_04623; -.
DR PATRIC; fig|566551.4.peg.4230; -.
DR HOGENOM; CLU_000422_4_0_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000014585; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 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; 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 NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 2.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 4: Predicted;
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}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 716 AA; 79337 MW; DDE8A29805C4AF75 CRC64;
MKKITSVCPY CGAGCKLKLV VENNKIIRAE AAEGVTNQNQ LCLKGYYGWD FLNDTKLLTP
RLTQPMIRYE KGGKLQPVSW EEAISYTAKR LKAIKEQFGP RAIMTTGSSR GTGNETNFVM
QKFARAVLNT NNVDCCARVC HGPSVAGLQA TLGNGAMSNS IGDIENSKCL LVVGYNCADS
HPIVARRVIK AKSNGAKIIV CDPRRIETAR IADQHLQIKN GCNMALVNAF GYVLLEEQLY
DKEYVAKYAE GLEAYRETVK GYAPEDVEHL TGIPAQQVRQ AMRTFAAAPS ATIMWGMGVT
QFGQAVDVVK GLSSLALLTG NLGRENVGVG PVRGQNNVQG ACDMGVLPNQ FPGYQDVVDP
EVRAKFAKAW GIDPAVMDDK VGVRITEVPH LAMEGKVKAY YIMGEDPLQT EADLGQVRKG
FEALDFVVVQ DIFMTKTAEV ADVLLPATSW GEHGGVFTCA DRGFQRFEKA IEPKYNVKRD
WEIISLLATE MGYPMHYEDN QQIWDELREL CPLFYGVTYE KMGDMGHVQW PCPTLDHPGT
PYLYKDSKFD TPTGKGQLFA AEWRAPAEVP DETYPLVLCT VREVGHYSCR SMTGNCAALQ
TLADEPGFMQ INPQDADELG IKNNQLVWVS SRRGKVISRA DVNERINKGS VYMTYQWWIG
ACNELTQDNL DPISKTPETK YCAVNVSAIE DQTWAENYAQ TTYNAMKARL REAVEA
//
