ID COBQ_ACAM1 Reviewed; 497 AA.
AC B0CCR3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 29-MAY-2013, entry version 43.
DE RecName: Full=Cobyric acid synthase;
GN Name=cobQ; OrderedLocusNames=AM1_4245;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA Mimuro M., Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by
CC glutamine, and one molecule of ATP is hydrogenolyzed for each
CC amidation (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain.
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DR EMBL; CP000828; ABW29225.1; -; Genomic_DNA.
DR RefSeq; YP_001518542.1; NC_009925.1.
DR ProteinModelPortal; B0CCR3; -.
DR STRING; 329726.AM1_4245; -.
DR EnsemblBacteria; ABW29225; ABW29225; AM1_4245.
DR GeneID; 5683048; -.
DR KEGG; amr:AM1_4245; -.
DR PATRIC; 20622594; VBIAcaMar40141_3919.
DR eggNOG; COG1492; -.
DR HOGENOM; HOG000224803; -.
DR KO; K02232; -.
DR OMA; AHTDLNP; -.
DR ProtClustDB; CLSK2475851; -.
DR BioCyc; AMAR329726:GCZJ-4232-MONOMER; -.
DR UniPathway; UPA00148; -.
DR GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:HAMAP.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:HAMAP.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR HAMAP; MF_00028; CobQ; 1; -.
DR InterPro; IPR017929; CobB/CobQ_GATase.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 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; Complete proteome; Glutamine amidotransferase.
FT CHAIN 1 497 Cobyric acid synthase.
FT /FTId=PRO_0000332315.
FT DOMAIN 250 445 GATase cobBQ-type.
FT ACT_SITE 331 331 Nucleophile (By similarity).
FT ACT_SITE 437 437 By similarity.
SQ SEQUENCE 497 AA; 54480 MW; 0AFACCCF3AC2D4AC CRC64;
MGAIMVVGTT SHAGKSIMAA VICRMLKRKG YQVTPFKGQN MALNAYVTNA GDEIGHAQAV
QAWAAGLEPR VEMNPILLKP QGDMTSQVIL NGKAVGRTQA ADYYRDYFDR GWQAITTALV
TLQQEFDWIV CEGAGSPAEI NLKHRDLTNM RVAKHLNAPT LLVADIDRGG VFAHIVGTLE
LLDPDERALI KGFVINKFRG QRSLLESGIT WLEERTGIPV VGVIPWLEHS LPAEDSLDLF
ERRRTKPNAE VTIAVIRLPR ISNFTDFDPL EAEPSVRLQF VGPNQPLGQP DAVIVPGSKT
TISDLQQLQV SSMADQLRAY SQAGGMVLGI CGGLQMLGQT ISDPMGTEGP PGEFAGLGLL
PLQTTMSGDK ITRQRQAQIT LPSDCSALGE DARTIQGYEI HQGQTQVLQP EAVQAWFDDP
ALGVVSCNHR ILGTYLHGIF NNGPWRRVWL NQLRAQKNLL PLPLAIPNYK VYRDHMLDQV
TDAIAPYLNL QPFLGKA
//
