COBQ_PROM0
ID COBQ_PROM0 Reviewed; 509 AA.
AC A3PE00;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=P9301_13521;
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
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; CP000576; ABO17975.1; -; Genomic_DNA.
DR RefSeq; WP_011863286.1; NC_009091.1.
DR AlphaFoldDB; A3PE00; -.
DR SMR; A3PE00; -.
DR STRING; 167546.P9301_13521; -.
DR EnsemblBacteria; ABO17975; ABO17975; P9301_13521.
DR KEGG; pmg:P9301_13521; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001430; 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..509
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002370"
FT DOMAIN 262..459
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 451
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 509 AA; 57487 MW; 9ED16BA9A3177890 CRC64;
MELEAKLHEI KKPIMVLGTS SGAGKSLTVT AICRILKNLG EEPIPFKGQN MSNNAWVDWE
GGEMAYSQAL QAFACGINPA AEMNPILLKP QGNSISEVIH LGKSIGTTTA KNYYKDWFTP
GWEVIKKSLK SIYEGNPNCR LIIEGAGSPV EMNLIHRDLT NLRVAKYLNA NCILVTDIER
GGVFAQIIGT LELMKPEEKK LIKGIIINRF RGDLSLFEDG KKWIENKTQI PVVGIIPWLN
DSFPPEDSLD LIEKKSLSKN PEIKVGIIKL PSISNFSDFD PLENEETIFI EWIRKSQNLS
KYDFIILPGS KQTIKDQIFL ENSGLSKDIR DYSKNKGNIV GICGGLQMLG TTLEDPYFKE
GSKNYSEQKI KGIGLLPLKT TFFKKKLTRQ IKSKSIWPCQ SEINGFEIHN GQTVLDEIQS
SLKINPIFED SDLGWYKENN KGGTIAGTYI HGIFENDSWR EHYINLIRKS KNLPTLNKKS
ISYKEKRQFI IDNLANEFHK HLNLKSFLS
