ID   COBQ_DEHMC              Reviewed;         503 AA.
AC   Q3ZXQ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=cbdbA890;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
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; AJ965256; CAI83027.1; -; Genomic_DNA.
DR   RefSeq; WP_011309378.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZXQ8; -.
DR   SMR; Q3ZXQ8; -.
DR   KEGG; deh:cbdbA890; -.
DR   HOGENOM; CLU_019250_2_2_0; -.
DR   OMA; EIHHGVA; -.
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; 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.
FT   CHAIN           1..503
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_1000002355"
FT   DOMAIN          251..450
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        442
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   503 AA;  54993 MW;  FC394A766E0EC845 CRC64;
     MAKLIMVQGT SSNVGKSILV TALCRIFKQD GYKVAPYKSQ NMALNAFVTK EGGEIGRAQA
     VQAEACGIEP SVDMNPILLK PEADSRSQII VNGKVDRTIS AREYYEYAPL LLDTALAALN
     RLREKNDIVV IEGAGSPAEI NLKQREIVNM RIAKEASAPV LLAGDIDRGG VFASLIGTID
     LLEPDERYYI KGYLINKFRG DASLLKPAID VLEDRTSIPV LGIIPYLRNM AIAQEDSVYL
     DECKGSLGET DLDIAVIRLP RISNYDDFDA LATDGASVRF VSKTAEIGNP DLIIIPGTKS
     TIPDMEYLEQ SGLAETIIKK ARKGTHVLGV CGGYQILGKM IYDPHKTESE TTELKGLGLL
     DTETTFEKEK ATTQISGQVK FDSGLLSGLA GCAVSGYEIH MGRTRLFSAQ PAFHITKTPK
     GPADYLDGAS NAEGTVLGTY IHGIFENAAF RRGFLNAIRR HKGIPERQAD YFDRDKEYDK
     LADIVRASID MEKIYAILNE GIR