ID A0A087ACW0_9BIFI Unreviewed; 701 AA.
AC A0A087ACW0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:KFI56610.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:KFI56610.1};
GN ORFNames=BCAL_0209 {ECO:0000313|EMBL:KFI56610.1};
OS Bifidobacterium callitrichos DSM 23973.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI56610.1, ECO:0000313|Proteomes:UP000029072};
RN [1] {ECO:0000313|EMBL:KFI56610.1, ECO:0000313|Proteomes:UP000029072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI56610.1,
RC ECO:0000313|Proteomes:UP000029072};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFI56610.1}.
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DR EMBL; JGYS01000001; KFI56610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087ACW0; -.
DR STRING; 1437609.BCAL_0209; -.
DR eggNOG; COG1391; Bacteria.
DR Proteomes; UP000029072; Unassembled WGS sequence.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR InterPro; IPR023057; GlnE.
DR InterPro; IPR005190; GlnE_rpt_dom.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 2.
DR Pfam; PF03710; GlnE; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KFI56610.1}; Transferase {ECO:0000313|EMBL:KFI56610.1}.
FT DOMAIN 24..152
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 287..531
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 555..698
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 701 AA; 79397 MW; 88F93D1B72CF9AC8 CRC64;
MDMTRPFVWT ASKRDNFVYD CQQMRKRVED LIPAPLKDRE IKLGRGGLRD VEFTVQMLQL
VHGRADETLR TRSTLESLAR LAEGGYVSRK QAARLSADYR FERVLEHRQQ MWALKRTHLF
PDLGATANLG GLERKRDVDV DALNQNQELR RVARAFHMHP EQLVERYDET RREVRHLHLD
IYYRPMLPVS AQLEDDQIDL SKTAAQERFS SIGFGDPDAA MRHVAALTSG IGRAAKINRI
ILPAVLEWLG QGQNPDMGLL NWRKLEEHFG TESEYLGFLR DSNSAAQRLC HVLSNSRFLG
DALNKSVESV TWLGDDERLR ARTRESLDVQ CRSSLERNSE NINDFATSMR AMRRHEIERI
GLAWMSGVMD DAASLKGMTD VYDAIIEASL EWAVGRRVRE GGLASAPAAL AVIGMGRYGG
REVNFSSDAD AILIYRPIPA GSGDIDEGTA NLFARKVVED LRAILQGPTT LEPQIELDLD
LRPEGKNGPL VRSYASCEEY YRSWASTWEH QALLRARYAA GDKELAHDFL ANIADPLRYP
HVDLTDTEIG DIRKLKARME AERLPRGVRR DRHLKLGKGG LSDVEWTVQL MQLEHAGDIA
DLRVNGTLPA LDVLEARKII SKADAFTLRR AWTMCTAARN GNYLWSGRAR QADILPDDMY
SLGGIAVYLG YDANRGQHFE NDLLAVMRKA REVTERLFYG R
//
