ID Q97GT6_CLOAB Unreviewed; 454 AA.
AC Q97GT6;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Heme biosynthesis (NirJ-2) family protein {ECO:0000313|EMBL:AAK80236.1};
GN OrderedLocusNames=CA_C2279 {ECO:0000313|EMBL:AAK80236.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80236.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK80236.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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DR EMBL; AE001437; AAK80236.1; -; Genomic_DNA.
DR PIR; A97181; A97181.
DR RefSeq; NP_348896.1; NC_003030.1.
DR RefSeq; WP_010965577.1; NC_003030.1.
DR AlphaFoldDB; Q97GT6; -.
DR STRING; 272562.CA_C2279; -.
DR GeneID; 44998756; -.
DR KEGG; cac:CA_C2279; -.
DR PATRIC; fig|272562.8.peg.2477; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_3_3_9; -.
DR OrthoDB; 9808591at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21124; SPASM_CteB-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR024025; SCIFF_rSAM_maturase.
DR InterPro; IPR047602; SPASM_CteB-like.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR NCBIfam; TIGR03974; rSAM_six_Cys; 1.
DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR PANTHER; PTHR43273:SF8; RADICAL SAM PROTEIN-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDG01216; thioether_bond_formation_requi; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; 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:UP000000814};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 91..323
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT COILED 39..71
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 454 AA; 52753 MW; 6E533E37A0C80791 CRC64;
MSLVHKFIQD DQRYIIDVNS GSIHEVDEMV YDLIDEDKIR SKKKLLDRLK NKYKEEEISE
AYDEIKELID EGVLYSKDLY EDIAKESTKS PSFIKALCLN IAHDCNLKCK YCFADEGEYK
GCREIMSPEV AKKSIDFVIK HSGPRKNIEV DLFGGEPLMA FDTIKQVVEY AKKEEKKYNK
NIRFTMTTNA TLLNDEIMDY LDKNMGNIIL SFDGRKEVND KVRVRADGTG SHDAILKNIK
KMVARRDKSK QYYVRGTFTR NNTDFFEDVK YIADMGFKEI SIEPVVLPDD HNLSLREEDI
PQIFEQYDKL YKDMIKRHKE GKEIKFYHFN IDINGGPCVY KRISGCGAGH EYVSITPSGD
VYPCHQFVGN EDFKMGTIYD DDNINKEMGN EFREAHIYNK PKCRECWARF YCSGGCQANN
YNFNGDMHIP YEIGCKMQKK RIECAIALKA QMVD
//
