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Database: UniProt
Entry: E1R8J2_SEDSS
LinkDB: E1R8J2_SEDSS
Original site: E1R8J2_SEDSS 
ID   E1R8J2_SEDSS            Unreviewed;       490 AA.
AC   E1R8J2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   OrderedLocusNames=Spirs_0179 {ECO:0000313|EMBL:ADK79336.1};
OS   Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS   (Spirochaeta smaragdinae).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Sediminispirochaeta.
OX   NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK79336.1, ECO:0000313|Proteomes:UP000002318};
RN   [1] {ECO:0000313|EMBL:ADK79336.1, ECO:0000313|Proteomes:UP000002318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC   {ECO:0000313|Proteomes:UP000002318};
RX   PubMed=21304743; DOI=10.4056/sigs.1143106;
RA   Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA   Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA   Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA   Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT   4228).";
RL   Stand. Genomic Sci. 3:136-144(2010).
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:0000256|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00028}.
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DR   EMBL; CP002116; ADK79336.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1R8J2; -.
DR   STRING; 573413.Spirs_0179; -.
DR   KEGG; ssm:Spirs_0179; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_12; -.
DR   OMA; EIHHGVA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002318; 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-UniRule.
DR   CDD; cd05389; CobQ_N; 1.
DR   CDD; cd01750; GATase1_CobQ; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR   InterPro; IPR004459; CobQ_synth.
DR   InterPro; IPR011698; GATase_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00313; cobQ; 1.
DR   PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR   PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   Pfam; PF07685; GATase_3; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51274; GATASE_COBBQ; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00028};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_00028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002318}.
FT   DOMAIN          1..231
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          248..440
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   490 AA;  53112 MW;  C542B867ACE8ADFC CRC64;
     MIQGTSSNVG KSLLVAAFCR IFARKGLRVF PFKSQNMALN SFVTSEGLEI GRAQALQATA
     AKRDAEVAMN PVLLKPEGNS SSQVVLMGKP WRRLSGGEYY KAKPALWETI TEVLDRAGKE
     NDLLIVEGAG SPAEINLKEH EIVNMRVARY LQAPVLLAAD IDRGGVFAFL YGTLALLEPE
     ERELVKGFII NKFRGDVELL KPGLDMLRNL TGGVPTLGVV PYLKEISLAQ EDSVFLEEHR
     FFGSGSTEIA VMLLPHISNY DDFDALTMEP GLQLRFVEHP RELGNPAAII LPGTKTTMAD
     LLWLRQSGLA EAICRKVEEG TSVIGICGGF QMLGRQIIDK EGVEGSAGSL RGLGLLDVTT
     YFSREKKTIQ ETGTLCSDKG TLAPMKGYKV SGYEIHMGHS ALGESAGPFL ATGSGGRDGA
     VSPDGRIIGT YFHGLFDEAA FRRGWLASLG WEPEGKPVSL VQRREEELEA LADAVEAAID
     MKQLEAIIGL
//
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