COBQ_PROMS
ID COBQ_PROMS Reviewed; 509 AA.
AC A2BS60;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-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=A9601_13371;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM70621.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000551; ABM70621.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041484551.1; NC_008816.1.
DR AlphaFoldDB; A2BS60; -.
DR SMR; A2BS60; -.
DR STRING; 146891.A9601_13371; -.
DR PRIDE; A2BS60; -.
DR EnsemblBacteria; ABM70621; ABM70621; A9601_13371.
DR KEGG; pmb:A9601_13371; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002590; 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.
FT CHAIN 1..509
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332361"
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; 57417 MW; 8BA10CAE40857433 CRC64;
MELEAKLHEI RKPIMVLGTS SGAGKSLTVT AICRILKNLG EEPIPFKGQN MSNNAWVDWE
GGEMAYSQAL QAFACGINPS AEMNPILLKP QGNSISEVIH LGKSIGITTA SNYYKDWFIP
GWEVIKKSLS SIYEKTPNCR LIIEGAGSPV EMNLIHRDLT NLRVAKYLNA NCILVTDIER
GGVFAQIIGT LELMKPEEKK LIKGIIINRF RGDLSLFAEG KKWIESKTQI PIIGIIPWLN
DSFPPEDSLD LLEKKSRHTT AEIKVGIIKL PSISNFSDFD PLENEKSILI EWVRESQNLK
KFDFIILPGS KQTIKDQIYL KESGLSQDIK EYSNNKGNII GICGGLQMLG TSLEDPFFKE
GSKSCLEQKI KGIGLLPLKT TFFEKKLTRQ ISSESLWPCH SKINGFEIHN GKTELVESEN
LLKIRPIFKD LDLGWYTEKK EGGTIAGTYI HGIFENDNWR DQYINLIRKS KNLPIFNKKS
ISYKKKRESI IDNLANEFDK HLNITSLLN
