COBQ_PHOPR
ID COBQ_PHOPR Reviewed; 492 AA.
AC Q6LIL7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-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=PBPRB0991;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378678; CAG22863.1; -; Genomic_DNA.
DR RefSeq; WP_011221058.1; NC_006371.1.
DR AlphaFoldDB; Q6LIL7; -.
DR SMR; Q6LIL7; -.
DR STRING; 298386.PBPRB0991; -.
DR EnsemblBacteria; CAG22863; CAG22863; PBPRB0991.
DR KEGG; ppr:PBPRB0991; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000593; Chromosome 2.
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..492
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141315"
FT DOMAIN 252..440
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 492 AA; 53267 MW; 7EAB7FDA8A52FBC9 CRC64;
MQLTTQALMV QGTTSDAGKS VLVTGLCRVL VRKGIKVAPF KSQNMALNSA VTKDGGEIGR
AQAVQAQAAC IEPTVHMNPV LLKPNTDVGA QIIVQGKAIA DMDAIGYNGY KKVVMGPIME
SFGILQDEYQ TVIIEGAGSP AEINLRENDV ANMGFAEKAD VPVIIIADID RGGVFAHLYG
TLALLSESEQ ARVIGFVINR FRGDIKLLES GLDWLEEKTG KPVLGVLPYL HGLMLEAEDA
INVQQVEAAD EQLNVVVPVL TRVSNHTDFD PLRMHPQVNL QFVGKGQPIP PTDLIIIPGT
KSVRSDLAFL REQGWDKQIE RHLRLGGKVM GICGGYQMLG ESIADPDGIE GDAGESQGLG
YLQTSTILAP EKQLKQTVGT LQLPEQPAVP VRGYEIHAGI TSGIQTNAPV QLQDGPDGQL
GIDNQVFGTY LHGIFEQTEA CNAILSWAGL EATQTPDFDL IREQGIDRVA DTLEEYMKLD
KLWPEWADKF AK
