ID   COBQ_ACIAD              Reviewed;         465 AA.
AC   Q43989;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Cobyric acid synthase;
GN   Name=cobQ; OrderedLocusNames=ACIAD1071;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9074511; DOI=10.1016/s0378-1119(96)00728-7;
RA   Geissdoerfer W., Ratajczak A., Hillen W.;
RT   "Nucleotide sequence of a putative periplasmic Mn superoxide dismutase from
RT   Acinetobacter calcoaceticus ADP1.";
RL   Gene 186:305-308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z46863; CAA86930.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG67958.1; -; Genomic_DNA.
DR   RefSeq; WP_004921625.1; NC_005966.1.
DR   AlphaFoldDB; Q43989; -.
DR   STRING; 62977.ACIAD1071; -.
DR   DNASU; 2877936; -.
DR   EnsemblBacteria; CAG67958; CAG67958; ACIAD1071.
DR   GeneID; 45233512; -.
DR   KEGG; aci:ACIAD1071; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OMA; DVRMNPL; -.
DR   OrthoDB; 744477at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04935-MON; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000430; 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..465
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141284"
FT   DOMAIN          249..417
FT                   /note="GATase cobBQ-type"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        409
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  52572 MW;  999E79BF28F879ED CRC64;
     MRHISIFGTS SDAGKSTLTF VIAKILQRAG IRVAPFKAQN VSNNARVCDD GSEIAIAQSF
     QAEVLAIPTS YHLNPILLKS GINGQASVIV EGQVISQQDV LEYYRDLDTL KPAVQRCFET
     LAKMYDCIVA EGAGSPVELN LMDKDLSNIF IAKHYQTKII LVADIEKGGV FASVWGTYNL
     LPADLRSNVI GVIINKFRGD LSLFDEGIRI IEQAFKIPVL GVLPYMPFNL GFEDNASLQN
     FVQQPRQKKL KIGVIAYPYM SNYNDFEPLI ADDEVLLEFI NSPISLEHFD GVILPGSKLV
     IEDLHWLKTN GLFEQLQQRR KPIFAICGGY EMLFEQLHDP ERIENLEPTT ATGLGLIDDE
     IYFAKNKILN KAEYPIFGLN IAGFEMHHGI SQKYPLYFQK DNIQGTFIHQ VFDHNAFRTQ
     YLRAICAQYQ GFDFQLYKTE QINNFIEACR KRLNVKLILE AIQDQ