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Database: UniProt
Entry: Q1N8J1_SPHSS
LinkDB: Q1N8J1_SPHSS
Original site: Q1N8J1_SPHSS 
ID   Q1N8J1_SPHSS            Unreviewed;       485 AA.
AC   Q1N8J1;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SKA58_10773 {ECO:0000313|EMBL:EAT07318.1};
OS   Sphingomonas sp. (strain SKA58).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT07318.1, ECO:0000313|Proteomes:UP000005395};
RN   [1] {ECO:0000313|EMBL:EAT07318.1, ECO:0000313|Proteomes:UP000005395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA58 {ECO:0000313|EMBL:EAT07318.1,
RC   ECO:0000313|Proteomes:UP000005395};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025166, 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|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAT07318.1}.
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DR   EMBL; AAQG01000022; EAT07318.1; -; Genomic_DNA.
DR   RefSeq; WP_009821914.1; NZ_CH959306.1.
DR   AlphaFoldDB; Q1N8J1; -.
DR   STRING; 314266.SKA58_10773; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_5; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000005395; Unassembled WGS sequence.
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:UP000005395}.
FT   DOMAIN          4..236
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          253..433
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   485 AA;  51187 MW;  E2366F170B1681CC CRC64;
     MGAIMLQGTG SDVGKSVLVA GLCRALRLRG HNVRPFKPQN MSNNAAVTVD GGEIGRAQAL
     QAIACGVPAH TDMNPVLLKP QADRSSQLIV HGQVRGTLGS GNFRAARGAL LDEVLESYHR
     LRGQCDIVVV EGAGSPAEIN LRAGDIANMG FARAADVPVI LVGDIDRGGV IAAVVGTRAV
     LDAADAAMIR GFLINKFRGD LSLFEDGYRQ IEERSGWRGF GVVPWLNAVA RLPSEDAVVL
     ERPVASIEAP IVIACPVLPR ISNFDDLDPL KLEPAVDLRM IGPGQPIPGD AALVILPGSK
     ATIADMLAMV EQGWDIDIRA HHHRGGAVLG LCGGYQMLGR TIRDPDGIEG SVREINGLGL
     LEVDTILAGA KTLEQVRGRA LTADFHGYEM HMGRTEGPGC ARPFAMLGNK PDGAISPDGR
     VMGSYVHGLL ASTQLRAALL QRIGATSAQA DYGRSVEDAL DALAAHLERH CDIDAMVALA
     RGENK
//
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