ID COBQ_SHEAM Reviewed; 496 AA.
AC A1S3L6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Sama_0765;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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=ABL98972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000507; ABL98972.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011758882.1; NC_008700.1.
DR AlphaFoldDB; A1S3L6; -.
DR SMR; A1S3L6; -.
DR STRING; 326297.Sama_0765; -.
DR KEGG; saz:Sama_0765; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000009175; 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; cd05389; CobQ_N; 1.
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; IPR047045; CobQ_N.
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; Reference proteome.
FT CHAIN 1..496
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332386"
FT DOMAIN 251..449
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 441
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 496 AA; 53039 MW; 4C610153B56ECFB1 CRC64;
MIQGTASDAG KTTLVAGLCR LLARQGLKVA PFKPQNMALN SAVTEDGGEI GRAQALQAAA
CGLKPHTDFN PILLKPGSDT RAQVIVHGKA LTSLEASAFF GPEGKGYKAI AIEAVLESYN
RLKQSFDYLL VEGAGSPAEI NLRENDIANM GFAEAVDCPV ILVADIDKGG VFAQLVGTLA
LLSESEQARI KGFVINRFRG DINLLQPGLD WLEAHTGKPV LGVVPYLHNL LLDAEDALVP
YQQAGADSGA RFRVRVLVYP RTSNHTDFDP LRLHPGVDFD YLDIQHASPD ALQGADLVIL
PGSKNVRADL ECLKTKGFDC ALRKHVRYGG KLVGICGGYQ MLGIEIDDPD GVEDTPGSSD
ALEFLPLITE LEGSKVLANV SGELSLGEEA VAVKGYEIHC GRTTVLGQLS RPLFLVDDTG
NPASDRGCIS DDGAIFGCYL HGIFDTPAAL DAVLAWAGYR GAARGTSLEE HREQQLERLA
DTLAEHLDMA RLNSLF
//
