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
//