COBQ_ACAM1
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 25-MAY-2022, entry version 80.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=AM1_4245;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
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., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA 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 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; CP000828; ABW29225.1; -; Genomic_DNA.
DR RefSeq; WP_012164556.1; NC_009925.1.
DR AlphaFoldDB; B0CCR3; -.
DR SMR; B0CCR3; -.
DR STRING; 329726.AM1_4245; -.
DR EnsemblBacteria; ABW29225; ABW29225; AM1_4245.
DR KEGG; amr:AM1_4245; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000268; 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; 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; Reference proteome.
FT CHAIN 1..497
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332315"
FT DOMAIN 250..445
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
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