ID A0A4P8YI31_9ENTR Unreviewed; 720 AA.
AC A0A4P8YI31;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:QCT20395.1};
GN ORFNames=FEM41_12415 {ECO:0000313|EMBL:QCT20395.1};
OS Jejubacter calystegiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Jejubacter.
OX NCBI_TaxID=2579935 {ECO:0000313|EMBL:QCT20395.1, ECO:0000313|Proteomes:UP000302163};
RN [1] {ECO:0000313|EMBL:QCT20395.1, ECO:0000313|Proteomes:UP000302163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSNA2 {ECO:0000313|EMBL:QCT20395.1,
RC ECO:0000313|Proteomes:UP000302163};
RA Jiang L., Jeong J.C., Kim C.Y., Kim D.H., Kim S.W., Lee j.;
RT "Complete genome sequence of Izhakiella calystegiae KSNA2, an endophyte
RT isolated from beach morning glory (Calystegia soldanella).";
RL Submitted (MAY-2019) 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};
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DR EMBL; CP040428; QCT20395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8YI31; -.
DR KEGG; izh:FEM41_12415; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000302163; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000302163}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 720 AA; 79667 MW; D5072224F74DF49C CRC64;
MKKITSVCPY CGAGCKLKLV VDNNRITRVE AANGVTNQNE LCLKGYYGWD FLNDTRLLTP
RLKQPMIRYR KDGPLEPVTW DEAIRYTAER LSDIKARYGS QAIMTTGSSR GTGNETNYVM
QKFARAVLNT NNVDCCARVC HGPSVAGLQQ TLGNGAMSNA IADIENSRCL LIFGYNCADS
HPIVARRVLK AKQRGARIIV CDPRKIETAR IADLHLQLNN GSNMALVNAF IHVLLEEELY
DRAWVARHTE GLEALRETVK NYAPESVEGI TGVPAAAIRQ AMRLYCAAPS ATVMWGMGVT
QFGQAVDVVK GLSSLALLTG NLGREHVGVG PVRGQNNVQG ACDMGVLPDH FPGYQRVDDP
RTRAKFAAAW GVDPAAMDNK IGVRITDVPH LALEGKIKAY YIMGEDPLQT EADLGLVRRG
IEALDLLIVQ DIFMTKTAEK ADVLLPATSW GEHGGIFTCA DRGFQRFEQA ITPRDDVRRD
WQIISQIASA MGYPMHYDSN QQIWDEMREL CPLFYGATWE KIGEMGHLQW PCPTLEHPGT
PWLYQGGRFD TPSGKGQLYA APWRPPAEQP DADYPLVLCT VREVGHYSCR SMTGNCAALQ
TLADEPGFVA IHPQDAAPLG IKEDHLVRVA SRRGEVFSRA RLSERVNPGA VYMTYQWWIG
ACNELTQDNM DPVSHTPETK YCAVRLLPIA DQDRAESEVL AAYSEMKARL RAAAEPVMQP
//