ID   COBQ_HERA2              Reviewed;         489 AA.
AC   A9AZZ2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Haur_1051;
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) 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; CP000875; ABX03699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AZZ2; -.
DR   STRING; 316274.Haur_1051; -.
DR   EnsemblBacteria; ABX03699; ABX03699; Haur_1051.
DR   KEGG; hau:Haur_1051; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_0; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000787; 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; Reference proteome.
FT   CHAIN           1..489
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000090229"
FT   DOMAIN          252..441
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        433
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   489 AA;  53562 MW;  8F6743D4EC36D79F CRC64;
     MLAPVLMVVG TASSVGKSTL VSALCRIAAR RGIRVAPFKA QNMSNNAAVT ANGEEIARSI
     AVQAAAAKLT PSVQMNPILI KPEGQRRSQI IVQGRPWQTL EAIDYWQRKQ LLWEIVTNSL
     DQLRQAYDLV IAEGAGSPVE LNLKAHDITN MRVATYAQAQ TLLVGDIDVG GIFAAMLGTL
     MLLEPEERQL IAGLIVNRFR GDPDLFTDGI QILEQRSNKP VLGVVPWLPQ LGLPEEDAVA
     LERPDQTTNN AALTIGVIQL PAIANFDDFD PLAQEQGVAV RYINQPHELQ HCQALILPGT
     KHTLAARQWL TEQGFDQAIQ QFQGPIVGIC GGYQLLGQQI DDPEAVEGIG GSMAGLGLLP
     ITTIFQRHKQ TRQVQALSNL PWAKAYPLAG YEIHMGRTEL LADQPAFSIQ QAESTHADGC
     MRANGKVWGC YIHGIFANTE FRQAWLSRLG WQVQSAIQPI DPFERLADHV EACLEPNLLT
     KLLGQEIRD