ID E9RSQ6_9FIRM Unreviewed; 509 AA.
AC E9RSQ6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=HMPREF0490_00300 {ECO:0000313|EMBL:EGC75659.1};
OS Lachnospiraceae bacterium 6_1_37FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658656 {ECO:0000313|EMBL:EGC75659.1, ECO:0000313|Proteomes:UP000006471};
RN [1] {ECO:0000313|EMBL:EGC75659.1, ECO:0000313|Proteomes:UP000006471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_1_37FAA {ECO:0000313|EMBL:EGC75659.1,
RC ECO:0000313|Proteomes:UP000006471};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_37FAA.";
RL Submitted (JAN-2011) 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|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}.
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:EGC75659.1}.
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DR EMBL; ADCR01000005; EGC75659.1; -; Genomic_DNA.
DR AlphaFoldDB; E9RSQ6; -.
DR STRING; 658656.HMPREF0490_00300; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006471; 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}.
FT DOMAIN 5..226
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 251..451
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 445
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 509 AA; 56046 MW; AC62B67CBA9119AF CRC64;
MAKAIMIQGT MSSAGKSLIA AGLCRIFRQD GYRCAPFKSQ NMALNSFITE DGLEMGRAQV
MQAEAAGIEP SVWMNPILLK PINDMGSQVI VNGEVIGTMK ARDYFAYKKQ LIPDILRAYQ
KLEAEYDIIV IEGAGSPAEI NLKQDDIVNM GMAKLAKAPV LLVGDIDRGG VFAQLLGTLL
LLEEEEKQMV KGLIINKFRG DKTILDPGVV MLEEKGGIPV VGVAPYLQVQ LDDEDSLTER
FWMKEAAGKI DIAVIRLPRI SNFTDFNALE VAKEASVRYV EHVRELQKPD LIILPGSKNT
MEDLRWLRES GMEAAILKAH AKGTVIFGIC GGYQMLGETI KDPEQMEAGG TIQGMGLLPV
DTVFSTEKTR TRVEGTFSMP GGTLKRLAGI PLYGYEVHMG QTVCRGQTLT KLQETSHKRE
AFQLEKEGEK ADGCWKENVY GTYVHGIFDG EGVVPAILEA LAEKKGITLS DLEQVDFAAF
KETQYNLLAE GLRAHLDMEK IYEILETGI
//
