COBQ_AROAE
ID COBQ_AROAE Reviewed; 489 AA.
AC Q5P3B0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=AZOSEA20790;
GN ORFNames=ebA3690;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR555306; CAI08204.1; -; Genomic_DNA.
DR RefSeq; WP_011237897.1; NC_006513.1.
DR AlphaFoldDB; Q5P3B0; -.
DR SMR; Q5P3B0; -.
DR STRING; 76114.ebA3690; -.
DR EnsemblBacteria; CAI08204; CAI08204; ebA3690.
DR KEGG; eba:ebA3690; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_4; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006552; 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_1000002345"
FT DOMAIN 251..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 489 AA; 51739 MW; 37B0893F87A673D4 CRC64;
MPHAVALMVQ GTTSDAGKST LVAGLARVLF RRGVRIAPFK PQNMALNSAV TVDGGEIGRA
QALQALAAGL EPHSDFNPVL LKPSTDVGAQ VVIHGRVALS LSARDYHAYK PTAMAAVMAS
WDRLVTAYEC VLVEGAGSPA EINLRDRDIA NMGFAEAADV PVILVADIDR GGVFAHLVGT
LELLSPSEQA RVKGFVINRF RGDLGLLQPG LDWLEARTGR PVLGVLPYLH GLFLDAEDAL
ADARAEKGET RLTVVAPVYP RISNHTDLDA LRLHPQVDFR WVGPGQAMPP ADLIVLPGSK
SVQADLAWLR AQGWDAAILR HLRYGGKLAG ICGGFQMLGG WLHDPLGLEG GAGSIAGLGL
LDMETTLAAE KRLENVCGTL NLPRSPAAAG YEIHMGVSRG AALDRPALQF ADGRGDGALS
ADGQILGTYL HGLFDTPAAL SALLAWAGAG EVESVDLAAR READLDRLAD AIERHLDLGR
LFPAEWVRG
