COBQ_MARMS
ID COBQ_MARMS Reviewed; 500 AA.
AC A6W1K0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Mmwyl1_3678;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000749; ABR72579.1; -; Genomic_DNA.
DR RefSeq; WP_012071344.1; NC_009654.1.
DR AlphaFoldDB; A6W1K0; -.
DR SMR; A6W1K0; -.
DR STRING; 400668.Mmwyl1_3678; -.
DR EnsemblBacteria; ABR72579; ABR72579; Mmwyl1_3678.
DR KEGG; mmw:Mmwyl1_3678; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
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.
FT CHAIN 1..500
FT /note="Cobyric acid synthase"
FT /id="PRO_1000074400"
FT DOMAIN 251..449
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 332
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 500 AA; 54677 MW; 55D4F455372AE115 CRC64;
MPAFSLMIQG TTSDAGKSTL VTALCRLFYR RGISVAPFKP QNMALNSAVT KDGNEIGRAQ
AVQAYAAGLE PQVDMNPILL KPNTDTGAQV IIQGKAVGNM NAVGYHEYKS IAKVAALDSY
QRLANQYQAV LIEGAGSPAE INLRARDIAN MGFAESIDCP VIIIADIDKG GVFAHLVGTL
DLLSPSEQDR VIGFVINRFR GDISLLQSGL DWLEERTGKP VLGVLPFLKG FHLESEDAVA
KSPIKADSKA KLNIVIPIMP RTSNHTDWDA LRLHPEVQVT LVGANETIPP ADLVILPGSK
SVQSDLAYLR QEGWEDYLNK HLRYGGKVIG ICGGYQMLGE QLLDPLGLEN QHANTRSTGF
GFIPMETVLK EEKQLKQRQG QLAFAANAQV TGYEIHSGVS RFTDETQIAH FALLDDGKNK
ENSEKEGYIS PDGQIIGTYL HGVFDHPDAL QALLNWAGVD QAAAFDYDQF RDKEIDRLAD
STEQNMNIDA LIEQCQNFQQ
