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Database: UniProt
Entry: C2MBK4_9PORP
LinkDB: C2MBK4_9PORP
Original site: C2MBK4_9PORP 
ID   C2MBK4_9PORP            Unreviewed;       472 AA.
AC   C2MBK4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Iron-only hydrogenase maturation rSAM protein HydG {ECO:0000313|EMBL:EEK16877.1};
GN   Name=hydG {ECO:0000313|EMBL:EEK16877.1};
GN   ORFNames=PORUE0001_0688 {ECO:0000313|EMBL:EEK16877.1};
OS   Porphyromonas uenonis 60-3.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=596327 {ECO:0000313|EMBL:EEK16877.1, ECO:0000313|Proteomes:UP000003303};
RN   [1] {ECO:0000313|EMBL:EEK16877.1, ECO:0000313|Proteomes:UP000003303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=60-3 {ECO:0000313|EMBL:EEK16877.1,
RC   ECO:0000313|Proteomes:UP000003303};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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:EEK16877.1}.
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DR   EMBL; ACLR01000123; EEK16877.1; -; Genomic_DNA.
DR   RefSeq; WP_007365215.1; NZ_ACLR01000123.1.
DR   AlphaFoldDB; C2MBK4; -.
DR   STRING; 596327.PORUE0001_0688; -.
DR   eggNOG; COG0502; Bacteria.
DR   OrthoDB; 9801120at2; -.
DR   Proteomes; UP000003303; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          276..383
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
SQ   SEQUENCE   472 AA;  53599 MW;  4784C916F849C62F CRC64;
     MSYNKQSHDA CDFINHDEII DTLRYAEQHK DDEKVISDIL RKATEMRGLD HREAAVLLLA
     EDPATRQRVS QLAEQIKLRF YGKRIVLFAP LYLSNYCING CVYCPYHAKN RTIPRHKLTQ
     EQIRQEVIAL QDMGHKRLAL EAGEDPRNNP IEYILESIQT IYSIHHKNGA IRRVNVNIAA
     TTVEEYRMLH EAGIGTYILF QETYHKEHYE ELHPRGPKSD YAYHTESMDR AMQGGIDDVG
     LGVLFGLSTY RYDFVGLMMH AEHLEATFGV GPHTISVPRI CPADDISLES FPEAIPDDTF
     LHIIAVARLA VPYTGIIVST REREAVRQRA LHVGVSQISG GSRTSVGGYA QTTEAAHSEQ
     FEVSDPRTLD EVVYWLLQQG HIPSFCTACY REGRTGDRFM SLCKSGQISN CCGPNALLTL
     QEYLEDYASP TTRELGLEMI SQQLPTVPNE RVRAIAQQRL QQIKAGERDF RF
//
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