COBQ_SYNS3
ID COBQ_SYNS3 Reviewed; 508 AA.
AC Q0IBR6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=sync_0893;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI46194.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0IBR6; -.
DR SMR; Q0IBR6; -.
DR STRING; 64471.sync_0893; -.
DR EnsemblBacteria; ABI46194; ABI46194; sync_0893.
DR KEGG; syg:sync_0893; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001961; 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..508
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332391"
FT DOMAIN 255..454
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 336
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 446
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 508 AA; 55278 MW; 79053E3A3D99811A CRC64;
MTAKPALMVL GTSSGAGKSL MTAALCRVLR RRGETPLPFK GQNMSNNAWV DQAGGEMAYS
QALQAWAAGL EPECAMNPVL LKPQGDSTSE LIHLGHSVGS ARAEHYYRDW FKPGWKAIRQ
GLEALQSSHP GGRLVLEGAG SPVEVNLQKR DLTNLRLAQY LRAHCVLVAD IERGGVFAQI
VGTLNLLRPV ERPLIKGLLI NRFRGRRELF DEGQRWLEAN TGVPVLGVMP WLDELFPPED
SLDLLERRGR KRSAELNIAV LKLPSLSNFS DLDPLEAEPT VQLRWVAPGE ELGLPDAVVI
PGSKQTLRDL AAILNSGLGA ALQAYNTGGG HVFGICGGMQ MLGDELCDPE GLEGGAPSGN
TSQAGLGLLP LRTVFSADKA LRQRSSAALW PGGSHALEIE GFELHHGLTT INNASETCKP
LCRDEELGWV KPFSDHGGLV AGTYLHGVFE SGPWRRRWLN QLRERKGLAP LSEQQPHHSR
QRDALLDRLA DAFEQHINLE PLLNSSNG