ID K8DX46_9FIRM Unreviewed; 491 AA.
AC K8DX46;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Iron-only hydrogenase maturation protein HydG {ECO:0000313|EMBL:CCO07005.1};
GN ORFNames=DESHY_10165 {ECO:0000313|EMBL:CCO07005.1};
OS Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO07005.1, ECO:0000313|Proteomes:UP000009315};
RN [1] {ECO:0000313|EMBL:CCO07005.1, ECO:0000313|Proteomes:UP000009315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT hydrothermale Lam5(T).";
RL Genome Announc. 1:e00114-e00112(2013).
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:CCO07005.1}.
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DR EMBL; CAOS01000001; CCO07005.1; -; Genomic_DNA.
DR AlphaFoldDB; K8DX46; -.
DR STRING; 1121428.DESHY_10165; -.
DR eggNOG; COG0502; Bacteria.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000009315; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR GO; GO:0042364; P:water-soluble vitamin biosynthetic process; IEA:UniProt.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR010722; BATS_dom.
DR InterPro; IPR024007; FeFe-hyd_mat_HydG.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR NCBIfam; TIGR03955; rSAM_HydG; 1.
DR PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR PANTHER; PTHR43583:SF2; BIOTIN AND THIAMIN SYNTHESIS ASSOCIATED DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF06968; BATS; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01060; BATS_domain_containing; 1.
DR SFLD; SFLDF00319; Fe_hydrogenase_maturase_(HydG; 1.
DR SMART; SM00876; BATS; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009315};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 281..402
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 491 AA; 56000 MW; 748EACC70F68FDC2 CRC64;
MSLMAINKAE IYHNQWEPAD FIKEEEINRM LEEAKQAPAA CVREIIEKAR QARGLTPEEV
AVLLQNEDEE LLSLMYEVAR EIKLKIYGKR LVLFAPLYIS DHCVNNCVYC GYRRDNKFKR
RKLTQEEVAE EVKILESMGH KRLALEAGEH PGECPIEYVL ECLNTIYSIK FDNGSIRRCN
VNIAATTIED YKKLKDAGIG TYILFQETYH RATYQKMHPS GPKADYDWHT TAHDRAMMAG
IDDVGFGVLF GLYDYKFEVL GLLMHALHLE ERFGVGPHTI SVPRLRPALG VDYNSFPYLV
NDDQFMKLVA IIRLAVPYTG MIISTRERPA YRDMLLNYGI SQISAGSCTG VGGYKRELQR
QQCLAEGGSR CGGEQDAPQF SVDDHRTPDE VLRSVCQSGW LPSYCTACYR KGRTGDRFMA
LAKSGEIQNV CQPNAILTFK EYLLDYASPE TRAVGEETIR RHLAEISNPQ IRKITEERLK
QIEAGERDLY F
//
