COBQ_CHLPB
ID COBQ_CHLPB Reviewed; 495 AA.
AC B3EJS3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=Cphamn1_1516;
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) 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; CP001101; ACE04442.1; -; Genomic_DNA.
DR RefSeq; WP_012474923.1; NC_010831.1.
DR AlphaFoldDB; B3EJS3; -.
DR SMR; B3EJS3; -.
DR STRING; 331678.Cphamn1_1516; -.
DR KEGG; cpb:Cphamn1_1516; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_10; -.
DR OMA; DVRMNPL; -.
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; 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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090222"
FT DOMAIN 253..446
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 438
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 53851 MW; 5D0C5DFF4DB61687 CRC64;
MRNLAVFGTA SDVGKSVVAT ALCRIFSNAG LDVAPFKAQN MSNNSGVTPD GLEMGRAQIV
QAEAARVVPT ADMNPVLLKP NTDTGAQVVL QGKAVANRSA RDYFGNTEVW AEAAFESLER
LTGRHDLVVI EGAGSCAEMN LYDRDFVNFR TAKEADAPVI LVADIDRGGV FAQVAGTLSV
IPPEDRARVK GVIINRFRGD SVLFDDGIRI LEELSGVPVL GVIPYFRGIH IEAEDAVPLQ
AVVDPAASPD PGKISIAIVY FPHISNFTDF AVFDLLDDAE VHYLHHPKDL ADYDAVILPG
SKNVRGDLDW MIFMGWKERL AEYRKRGGII AGICGGYQML GISVADPHGL EGEPGETSGL
GLLPVHTLLK KEKQLFNAKG CLFDDTIPVE GYEIHMGETR LTGKASPLLQ LTARNNRHSS
DTDGVISHDE KVFGTYFHGI FDGSAFRGWF LGKLRPDSAV NDTITEKDTE YNRLAEHFLS
HLNMGKVYEI IGRGK
