COBQ_HAHCH
ID COBQ_HAHCH Reviewed; 496 AA.
AC Q2SNC4;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=HCH_00962;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC27850.1; -; Genomic_DNA.
DR RefSeq; WP_011394925.1; NC_007645.1.
DR AlphaFoldDB; Q2SNC4; -.
DR SMR; Q2SNC4; -.
DR STRING; 349521.HCH_00962; -.
DR PRIDE; Q2SNC4; -.
DR EnsemblBacteria; ABC27850; ABC27850; HCH_00962.
DR KEGG; hch:HCH_00962; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000238; 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..496
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332340"
FT DOMAIN 250..437
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 429
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 496 AA; 54237 MW; C22F7DFD9E3D8711 CRC64;
MTNKTLMIQG TTSDAGKSTL VTAICRSLLR RGVKVAPFKP QNMALNSAVT VDGGEIGRAQ
AVQAQACGLQ PHTDMNPVLL KPNTDIGAQV IIHGKARANM DAVAYHDYKR TAMQAVLESF
QRLSSAYDAV LVEGAGSPAE INLRDRDIAN MGFAEEVDCP VILVADIDRG GVFAHLVGTL
ALLSESEQRR VRGFVINRFR GDIALLEPGL RWLEEYTGKP VLGVLPYLNG LHLEAEDALP
RDSIVKSDAT LKVIAPALPR ISNHTDFDPL RLHPQVDFQF IGPGQSPPPA DLIILPGSKS
VRNDLQWLRE NGWEEVIRKH LRYGGRVIGI CGGYQMLGRS IADPHGLEGV AGESVGLGWL
DIATTLEPEK QLRRVEGRLW LDDARITGYE IHAGVTRCLA SQTSAVCLED GRLDGVVSDD
NQVLGLYLHG LFESPQALTA LLRWAGLNEV QRLDYDALRE ADINRLADVV DQYLNWEEIA
GFLQVGPNSD DRESRA
