COBQ_CLONN
ID COBQ_CLONN Reviewed; 505 AA.
AC A0Q0K2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=NT01CX_2081;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61961.1; -; Genomic_DNA.
DR RefSeq; WP_011722154.1; NC_008593.1.
DR AlphaFoldDB; A0Q0K2; -.
DR STRING; 386415.NT01CX_2081; -.
DR EnsemblBacteria; ABK61961; ABK61961; NT01CX_2081.
DR KEGG; cno:NT01CX_2081; -.
DR PATRIC; fig|386415.7.peg.1186; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008220; 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..505
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002352"
FT DOMAIN 251..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 332
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 505 AA; 56501 MW; A2A3D2B348D6982F CRC64;
MKSKSIMVQG TASSVGKSIL CTGLCRVFYK DGYNVNPFKS QNMSLNSAIT CDGGEIGRAQ
YMQAEASNKV PSVKMNPILL KPNSDRGSQV IINGKVFKNM DAVDYYKFKP QLKKDVSKIY
NKLSDESDII VIEGAGSPAE INLNKEDFVN MGMAKIAKSP VILVGDIDKG GVFASIVGTM
MLLKEDERKM VRGVIINKFR GSYEILKPGL KMLEDIIKVP VLGVIPYFNL NLEDEDSATD
WSKFNFNSKG DIDVAVIKLP HMSNFTDINP LKMYDDVSIR LIEKVEDLKN PNLIIIPGSK
NTIKDMEYLK SSGMNSAILN CHSNGSFVFG ICGGFQILGS KIKDPNNIES NITSIEGLNL
INSVTEIKTD KTTTLTEARD KIFNCNIKGY EIHMGKTLID DNNSNFLVIN SRNEETCNDI
DGAISKDKRV FGTYIHGIFD NSEFTRKFLN LIRKNAGMDE IKETPKDYWE FKNEEYDKLA
DIIRNNVDMK KLYEIVNEGI DETDN
