COBQ_ALISL
ID COBQ_ALISL Reviewed; 495 AA.
AC B6ES52;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=VSAL_II0783;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178380; CAQ81537.1; -; Genomic_DNA.
DR RefSeq; WP_012552071.1; NC_011313.1.
DR AlphaFoldDB; B6ES52; -.
DR SMR; B6ES52; -.
DR STRING; 316275.VSAL_II0783; -.
DR EnsemblBacteria; CAQ81537; CAQ81537; VSAL_II0783.
DR KEGG; vsa:VSAL_II0783; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; GREVHDP; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001730; 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; 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..495
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090218"
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; 53841 MW; F70BB3C3394A544D CRC64;
MNTFAPLMVQ GTTSDAGKTV LVAGLCRVLS NKGIQVAPFK PQNMALNSAV TEDGGEIGRA
QALQADAARV KPHVHMNPIL LKPNTDIGAQ VIVQGKAIET MDAWGFQDYK KLAMPYVLES
FAYLNDHYQC VVVEGAGSPA EINLRENDIA NMGFAEAADV PVIIVADIDR GGVFAHLYGT
LALLSESEQA RVKGFVINRF RGDISLLVPG LEWLEEKTGK PVLGVIPYLH GLNLEAEDAI
KSEQQEKGQF VVKVPVVTRI SNHTDFDSLR LHPDIDLQFV GKGQSLSGAD FIILPGSKSV
QADLNYLRSQ GWDKDIERHL RFGGKVMGIC GGYQMLGEQL SDPLGIEGEP SLIDGLGHLA
ISTELKKQKQ LTLVEGELHL PNQSSAKVKG YEIHAGVSIH TAGAHLPVII NSESIVRYDG
ALNHEGSIFG TYLHGIFDEP EAFEAIMSWA GLKESKAIDM KEIQEEAIER IAASIEESLD
LSQLWPSLFE KKAAY