COBQ_GEOTN
ID COBQ_GEOTN Reviewed; 500 AA.
AC A4INZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=GTNG_1684;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO67048.1; -; Genomic_DNA.
DR RefSeq; WP_011887470.1; NC_009328.1.
DR AlphaFoldDB; A4INZ4; -.
DR SMR; A4INZ4; -.
DR STRING; 420246.GTNG_1684; -.
DR EnsemblBacteria; ABO67048; ABO67048; GTNG_1684.
DR KEGG; gtn:GTNG_1684; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001578; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
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; PF01656; CbiA; 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.
FT CHAIN 1..500
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002358"
FT DOMAIN 255..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 500 AA; 54925 MW; 29298C8935AC312F CRC64;
MAKTLPIMFQ GTHSDAGKSV IATAFCRMFA QDGWKTAPFK SQNMSLNSYV TPDGNEIGRA
QGIQAEAAGV AARAEMNPIL IKPSREHESQ IVVLGKPYGN MQAFAYRNEF FHQGLAVIRQ
SLETLMNEYD RIVIEGAGSP AEVNLNDREL VNMRVARLAN APVVLIGDIE RGGVFASLVG
TLALLEPEDR KRVVGVIINK FRGDAALLKP GLDWFEQYTG VPVLGVVPHL PDLAIDAEDS
LALERFAASS DDKGAIDIAV IRCPKIANFT DIDPLLTEPD CRVRLVTHAG ELGEPDVIVL
PGSKNTIEDL MYMKKRGLAS RIVSLVNEGK TTVVGLCGGY QMLGDVIRDP HGVETPFPEV
KGLGLLPVAT TLERTKTTVR SEGMLTWAGE RFSVRGYEIH MGRSTPLPGY VPLIEIGGRG
EGAKREDGRV LGTYMHDLFH NDAFRTAFFN VIRREKGLAS SAVRPFHSLK EAAFDRLAAH
VRQHVAVERI EQMMRQFQQR
