ID A0A090BW73_9GAMM Unreviewed; 476 AA.
AC A0A090BW73;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cobyrinic acid a,c-diamide synthase {ECO:0000313|EMBL:BAP58106.1};
GN ORFNames=THII_3809 {ECO:0000313|EMBL:BAP58106.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP58106.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP58106.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|ARBA:ARBA00006205}.
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DR EMBL; AP014633; BAP58106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090BW73; -.
DR STRING; 40754.THII_3809; -.
DR KEGG; tig:THII_3809; -.
DR HOGENOM; CLU_022752_2_1_6; -.
DR OrthoDB; 9764035at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05388; CobB_N; 1.
DR CDD; cd03130; GATase1_CobB; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004484; CbiA/CobB_synth.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00379; cobB; 1.
DR PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR Pfam; PF13500; AAA_26; 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 Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00606};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623}.
FT DOMAIN 250..441
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
SQ SEQUENCE 476 AA; 52945 MW; D7D8445F39C86E43 CRC64;
MPYFLISAAH KSSGKTTITL GLCAAFTRRG LVIQPFKKGP DYIDPLWLSQ AAQRPCHNLD
FQIMTPAEIQ RNVAWYSRDA DLCIIEGNMA FYDGIDLEGS NSNAALAKLL QAPVILVLDT
HGMTRSIAPL LLGYQAFDPE VYIAGVILNL VGGTRHESKL RATIEHYTDI PVIGAVQRDP
SIIIAERHLG LIPSYEASQA QTKINTIVNR ITDQIDLTHL IKIAQQAPKL PLVSQEILPP
TPLSTQSAIK IGIIRDAAFG FYYPGDLAAL ETGGAQLIFI DALHDSHLPP VDGLFIGGGF
PEVHMEKLSQ NHTLKQDIRN AIEQSMPVYA ECGGLMYLAR QLTWQEKTCD MVGALPFDTI
MTSRSQGRGY VYLRETGQGL WPLRDVSGQP TVFHAHEFHH SQVINLPTHL PFAYEVLRGH
GLDGQHDGII YKNTLANYAH LRDVENNHWT QRFIKFIRQC NQLPAPSFPH PLCQIE
//
