COBQ_MARN8
ID COBQ_MARN8 Reviewed; 489 AA.
AC A1TXB6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Maqu_0279;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM17385.1; -; Genomic_DNA.
DR RefSeq; WP_011783833.1; NC_008740.1.
DR AlphaFoldDB; A1TXB6; -.
DR STRING; 351348.Maqu_0279; -.
DR EnsemblBacteria; ABM17385; ABM17385; Maqu_0279.
DR KEGG; maq:Maqu_0279; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000998; 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.
FT CHAIN 1..489
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332345"
FT DOMAIN 247..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 489 AA; 52071 MW; AD31E855D51790A2 CRC64;
MPTLMVQGTT SDAGKTTVVA ALCRWLARQG VSVAPFKPQN MALNSAVTVD GGEIGRSTAL
QALACGLEPH SDMNPVLLKP QSDCGAQVIL RGKVHGNMDA LDYHAYKAEA MNSVMASWRD
LSARYDVVIA EGAGSPAEIN LRANDIANMG FAEAADCPVL LVGDIDKGGV FAQLVGTLAL
ISDSERGRTA GFVINRFRGD IALLEPGLDW LTEHTGKPVF GVLPYLHGLV IDSEDSVSAA
GTSEAGALKV VVPVLPRISN HNDFDPLRLH PGVDLVFVGT DEPIPPADLI ILPGSKSTRH
DLQWLKQQGW PEAIQKHLRY GGKLLGICGG FQMLGLKVED PEGLEGEVGT TKGLALFEMV
TRMVPGKQLR MVNGGLTSHV ASTAVTGALK GYEMHNGVTE GAALVRPFAE LEGRPDGAVS
ADGQVAGTYI HGVFDEPAAC KAILAWAGLK TQGEQSVDYQ RHRLQQLDRL ADQVDQCLDT
DRLRSLLQL
