COBQ_CROS5
ID COBQ_CROS5 Reviewed; 494 AA.
AC B1WYU3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=cce_3359;
OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS ATCC 51142)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX NCBI_TaxID=43989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51142 / BH68;
RX PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT important in the marine nitrogen cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(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; CP000806; ACB52707.1; -; Genomic_DNA.
DR RefSeq; WP_009545468.1; NC_010546.1.
DR AlphaFoldDB; B1WYU3; -.
DR STRING; 43989.cce_3359; -.
DR EnsemblBacteria; ACB52707; ACB52707; cce_3359.
DR KEGG; cyt:cce_3359; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_3; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001203; Chromosome circular.
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..494
FT /note="Cobyric acid synthase"
FT /id="PRO_1000090227"
FT DOMAIN 249..443
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 494 AA; 54892 MW; B67AC8571211D419 CRC64;
MKAMMVVGTT SHAGKSFITT AICRILARRG WHITPFKGQN MALNAYVTTT GGEIGYAQAV
QAWAAGINPR VEMNPILLKP QGNMTSQVIL GGKAAGITTA TNYYEQYFDK GWNMIVHSLE
RLAVEYDFVV CEGAGSPAEI NLKHRDLTNM RVAKYLNAPT LLVVDIDRGG AFAHVVGTLQ
LLDESERALI KGIVINKFRG QRSLLDSGIE WLENYTGIPV LGVIPWREIS FSAEDSLDLL
ERRRKEQKEI NVTILRLPHI ANFTDFEPLD AEKTVSISYL DLNEPLGYPD AVIIPGSKTT
INDLIALHES GIAKQLQDYV AAGGIVLGIC GGFQMLGEMV FDPDQLEGNN VSYAGLNLLP
IETVITPEKI VRQRHTCSVY PYPGFPITGY EIHQGVTRSS KSPHQRIKTT NHPLFEDGSL
GIVNDNQSVW GCYLHGIFDN GAWRRNWLNY LRNRRGLPSL PTGIANYREQ RETVLNQLAD
LVEQYIDLTP LLNN