COBQ_CHLCH
ID COBQ_CHLCH Reviewed; 506 AA.
AC Q3ARV1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Cag_1012;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000108; ABB28274.1; -; Genomic_DNA.
DR RefSeq; WP_011362039.1; NC_007514.1.
DR AlphaFoldDB; Q3ARV1; -.
DR SMR; Q3ARV1; -.
DR STRING; 340177.Cag_1012; -.
DR PRIDE; Q3ARV1; -.
DR EnsemblBacteria; ABB28274; ABB28274; Cag_1012.
DR KEGG; cch:Cag_1012; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_10; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
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..506
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332326"
FT DOMAIN 260..453
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 341
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 445
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 506 AA; 55308 MW; 426AF575DFF679F0 CRC64;
MVTPTKTYRS LAILGTASDV GKSIVATALC RIFRNAGIDV APYKAQNMSN NSGVTPDGLE
IGRAQIAQAE AACVVPTADM NPVLLKPNTD IGAQVVLQGR VCSNESAQGY FRDTSRWAEA
ARESLLRLKQ KHELLVIEGA GSCAEMNLYP RDFVNFRTAR EADAAVILVA DIDRGGVFAQ
VVGTLAVIPP EDRALVKGVI INRFRGDSEL FREGITMLEE MSGVPVLGVI PYFRHFAIDA
EDAVPLSAKV DPAQEPETGK VGVAAIYFPH ISNFTDLSPL EHDPSVTLHY LHHPKPLSAY
KVLILPGSKN VRGDYAWLQQ MGWEKEIRAF REAGGLVIGI CGGYQMLGCS IADPYGVEGE
SGTTQTLGLL ETETLLEQEK YLANSEGVLV GTSIKAFGYE IHNGRTTVGA NCHPLMNIVA
RNNHPESDVD GVVSADGRVI GTYFHGIFNE PAVKQWFLQQ ADSTYTLQPH ERGRQESYEL
LADHFRQHLD VNKLFELIDY EQSLLP
