ID COBQ_PROM9 Reviewed; 509 AA.
AC Q319X7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=PMT9312_1259;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RX PubMed=16556843; DOI=10.1126/science.1122050;
RA Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA Delong E.F., Chisholm S.W.;
RT "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL Science 311:1768-1770(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; CP000111; ABB50318.1; -; Genomic_DNA.
DR RefSeq; WP_011376805.1; NC_007577.1.
DR AlphaFoldDB; Q319X7; -.
DR SMR; Q319X7; -.
DR STRING; 74546.PMT9312_1259; -.
DR KEGG; pmi:PMT9312_1259; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002715; 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; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00313; cobQ; 1.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_1000002372"
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; 57798 MW; 75BB5C76B5D20FC7 CRC64;
MYLEEKLHKI KKPIMVLGTS SGAGKSLTVT AICRILKNLA EQPIPFKGQN MSNNAWVDWE
GGEMAYSQAL QAFACGVNPS SEMNPILLKP QGNSVSEVIH LGKSIGTTSA KNYYQDWFIP
GWEVIKKSLN SIYKKNPNCR LIIEGAGSPV EMNLKHRDLT NLKIAKYLKA NCILVTDIER
GGVFAQIIGT LELMKPEEKK LIKGIIINRF RGDLSLFEEG KKWIEEKTQI PVIGIVPWLN
DSFPPEDSLD LLENKSRFTN AEIKVGIIKL PSISNFSDFD PLENEESILI EWIRESQNLK
KYDFIILPGS KQTIKDQMFL EKTGLSHDLR EYSNNKGHII GICGGLQMLG TFLEDPFLKE
GSKTFSEQKI KGIGLLPLRT TFFEEKLTRQ ISSESLWPCQ SKINGFEIHN GQTELDNTQN
SLKINPIFKD LNLGWYKENK EGGTIAGTYI HGIFENDIWR DQYINLIRMN KKLPALKKRT
SSYKNKREKI IENLANEFNK HLNLSSLLN
//
