COBQ_CALS4
ID COBQ_CALS4 Reviewed; 508 AA.
AC Q8RCP3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=TTE0376;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; AE008691; AAM23663.1; -; Genomic_DNA.
DR RefSeq; WP_011024820.1; NC_003869.1.
DR AlphaFoldDB; Q8RCP3; -.
DR SMR; Q8RCP3; -.
DR STRING; 273068.TTE0376; -.
DR EnsemblBacteria; AAM23663; AAM23663; TTE0376.
DR KEGG; tte:TTE0376; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..508
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141337"
FT DOMAIN 249..451
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 443
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 508 AA; 57010 MW; 88F5979781A84663 CRC64;
MALKLMIQGT ASSVGKSLIV TALCRIFKQD GLKVAPFKSQ NMALNSYITE EGLEIGRAQA
VQAEAAGIKP SYHMNPILLK PSSDKKSQVV LRGRVYENMS AEEYFKFRPK LLELIKEDFD
FLAKRNDVVV IEGAGSPAEI NLKEKDIVNM GLAELVNAPV LLVGDIDRGG VFASIAGTML
LLDEKERNRV EGVIINKFRG DIEILKPGLK MLENIIQKEV LGVIPYMDVH IDEEDGATDR
FYTKCAQGEV DVAIINLPHI SNFTDFDPLT KVPGVKIKYV NKGERIGDCD VLIIPGTKNT
IGDLKVLKDY GLDKEILNLR EKGKFIVGIC GGFQMLGKVI KDPYHIESDT EEMEGLGLLS
IETVIEREKT TSETKAFLGE ELPDTLSSLK GLFVTGYEIH MGESYILGKG KHFSIVVERN
KEKVKVLDGA VSEDGRVFGT YIHGIFENSL FTKEFINIVR KEKGLTPLEE VINYREFREK
EYDRLANIVR NSLDMERIYQ IMERYRDK