COBQ_ALIF1
ID COBQ_ALIF1 Reviewed; 495 AA.
AC Q5E0T7;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=VF_A0289;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW87359.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000021; AAW87359.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_047863633.1; NC_006841.2.
DR RefSeq; YP_206247.1; NC_006841.2.
DR AlphaFoldDB; Q5E0T7; -.
DR SMR; Q5E0T7; -.
DR STRING; 312309.VF_A0289; -.
DR EnsemblBacteria; AAW87359; AAW87359; VF_A0289.
DR KEGG; vfi:VF_A0289; -.
DR PATRIC; fig|312309.11.peg.2893; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000537; Chromosome II.
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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141339"
FT DOMAIN 249..442
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 434
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 54245 MW; 4233CBD8468CC263 CRC64;
MRKYSPLMVQ GTTSDAGKTV LVAGLCRLLA NKGIQVAPFK PQNMALNSAV TEDGGEIGRA
QALQADAARV KPHVHMNPIL LKPNTDIGAQ VIVQGKAIET MDAWGFHDYK KLAMPYVLES
FSYLSNNYEC VVIEGAGSPA EINLRENDIA NMGFAEAADV PVIIVADIDR GGVFAHLYGT
LALLSESEQA RVKGFVINRF RGDISLLVPG LEWLEEKTGK PVLGVIPYLH GLNLEAEDAI
KSEQLDKGKF IVKVPVVTRI SNHTDFDPLR LHPEIDLQFI GKGDSLSGAD FIILPGSKSV
QADLEYIKSQ GWDKDIERHL RYGGKVMGIC GGYQMLGEHL ADPLGIEGVP CRVKGLGYLS
ISTELQKQKQ LTLVEGTLAL PNQNAVKVKG YEIHAGVSTN LGKEHIPISI HTKDAMRYDG
TINDENSIFG TYLHGVFDEP EAFEAILTWA GLEKCQAINM HDIQEEAIER IAKSMEDSLD
LSLIWPDVFE KNKAY