COBQ_MYCPA
ID COBQ_MYCPA Reviewed; 497 AA.
AC Q73VS8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, 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=MAP_2933c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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; AE016958; AAS05250.1; -; Genomic_DNA.
DR RefSeq; WP_003875118.1; NC_002944.2.
DR AlphaFoldDB; Q73VS8; -.
DR SMR; Q73VS8; -.
DR STRING; 262316.MAP_2933c; -.
DR PRIDE; Q73VS8; -.
DR EnsemblBacteria; AAS05250; AAS05250; MAP_2933c.
DR KEGG; mpa:MAP_2933c; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_11; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000580; 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; 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..497
FT /note="Cobyric acid synthase"
FT /id="PRO_0000141311"
FT DOMAIN 257..431
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 497 AA; 52912 MW; 5F699A54E6864647 CRC64;
MSGALLVAGT SSDAGKSVVV AGLCRLLARR GVRVAPFKAQ NMSNNSAVTV EGGEIGRAQA
IQARAAGLEP SVRFNPILLK PGSDRTSQLV IKGQVAESVT ATSYVQHRDR LAALVLNELT
CLRDEFDAVI CEGAGSPAEI NLRATDLANM GLARAADLAV ILVGDIDRGG LLAHLFGTVA
VLDPQDQALI AGFVVNKFRG DPALLQPGLR RLHDITGRPT YGVLPYADRL WLDAEDSLSV
LAHRVVGAPD PPLGDDWLRV AAVRLPRISN STDVEALACE PGVLVRWVSE PSDVADADLV
VIPGSKATVA DLSWLRERGL AAAITAHAAA GRPVLGICGG FQMLCRRIDD RVESGAGEVA
GLGLLDADIA FHPAKTLRRW QRPLAGYEIH HGRVSRCAEH SWFDSDAEPQ GLVRGAVFGT
HWHGLLDNDD FRRAWLVRVA DAAGRRFVPG DTDVAARRDA QLDLAADLLA AHLDVDAVLG
LLDGPPPRPR LATRLCR
