COBQ_PROM3
ID COBQ_PROM3 Reviewed; 506 AA.
AC A2C7X7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-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=P9303_08361;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM77587.1; -; Genomic_DNA.
DR AlphaFoldDB; A2C7X7; -.
DR SMR; A2C7X7; -.
DR STRING; 59922.P9303_08361; -.
DR EnsemblBacteria; ABM77587; ABM77587; P9303_08361.
DR KEGG; pmf:P9303_08361; -.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR BioCyc; PMAR59922:G1G80-753-MON; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002274; 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.
FT CHAIN 1..506
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332363"
FT DOMAIN 258..455
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 447
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 506 AA; 55920 MW; 7140CEBD4620FB87 CRC64;
MSTDGMSTPL MVLGTSSGAG KSLMSAALCR LLLRRGETPI PFKGQNMSNN AWVDESGGEM
AYSQALQAWA AGLKPQCAMN PVLLKPQGDS TSEVIHLGQS VGTARAETYY EQWFRPGWSV
IREALKDLQC SYTHGRLVLE GAGSPVEVNL QRRDLTNLRL AQFLRARCLL VADIERGGVF
AQIIGTLSLL KPVEKQLIRG LLINRFRGRR ELFDEGRDWL EAETGIPVIG VMPWLEELFP
PEDSLDLLER RGKKNDAEIE IAVLKLPSLS NFSDLDPLEA EPTVQLRWVE PGTFLGTPDA
VIIPGSKQTL RDLNSLNRSG LGSQLQTYAQ SGGHVFGICG GMQMLGRTLA DPLGLEGVTT
TDPSSSMAGL NLLPLDTVFK RSKALKQCQR ITQWPDNAKV KGFELHHGNS QLIQGSHESV
LPMADDPSLG WVSKNERCGQ VAGTYLHGIF ENGRWRRLWL NLIRKQKGLA DLPTDIPHHE
QQREQLLNRL TDVFEEHVNI NPLLGT