ID A0A261F649_9BIFI Unreviewed; 1032 AA.
AC A0A261F649;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamine-synthetase adenylyltransferase {ECO:0000313|EMBL:OZG54503.1};
GN ORFNames=ALMA_0964 {ECO:0000313|EMBL:OZG54503.1};
OS Alloscardovia macacae.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Alloscardovia.
OX NCBI_TaxID=1160091 {ECO:0000313|EMBL:OZG54503.1, ECO:0000313|Proteomes:UP000243657};
RN [1] {ECO:0000313|EMBL:OZG54503.1, ECO:0000313|Proteomes:UP000243657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24762 {ECO:0000313|EMBL:OZG54503.1,
RC ECO:0000313|Proteomes:UP000243657};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG54503.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWWT01000005; OZG54503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261F649; -.
DR Proteomes; UP000243657; Unassembled WGS sequence.
DR GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
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; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
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:OZG54503.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243657};
KW Transferase {ECO:0000313|EMBL:OZG54503.1}.
FT DOMAIN 111..339
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 360..470
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 623..858
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 884..1027
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 1032 AA; 115629 MW; 426C5CD9D5F79AE8 CRC64;
MSEDTASLST SDLIRAGFTS VSRAGRDVER LRLTLDALEK TGNAASWSLD DFLRVCSRVD
DPDGAVWHVA DVAEKLAEKF AEKGLDAAGS AASSTDPARA FFSASIDELS RIVALCGVSD
FLGRILSARP ELLFDVLDGA LPQFDYDIDF SGSYAQQVQY VRTVYWRNLL HIATDDAVSE
TPLEIQPVIS KRLSALIDAT LRAALRVAYA KVPASGGCRF AVFAMGKLGA QEINYISDVD
LVYIVDKSPE FQGDLTALGT QIGSVLHTVC SGIVPGVDVP ALWDIDTALR PEGKAGALVR
TVESAQAYYE NWAENWEFQA LLKARFVAGD ADVARAFSQM IEPLIWSASA RPNFVYDCRA
MRTRVEQLIP LDQKDREIKL GKGGLRDVEF TVQMLQLVHG RTDESLRIRG TLDALKLLAH
GGYINRQQAR ALSEDYRFLR VLEHRQQLKS MKRTHLFPKI SSVQEDIFTR SRHVSERDIA
QNADIVRLSR AVSLTPVQLV ERFDSVRREI RHLHMDIYYR PMLPNISQLS DDDITLSEDA
MRERFESVGF ADPEAAMRHV ESLTSGISRS SRINRILLPT VLLWIGSGQN PDMGLMMWRR
WVDTFGGSGP YLGFLRDSPT ALRRMCHILS NSRYLSDALM KSSESTFWLG DDVALQPRST
ASLRTRTNVM LTRFSSLDTQ NEFATLLRAL RRREIERVGL GWMSSVISSE DALHAMTRVY
DVLIDAAVRW AAAVSGPSAP ARLSVIAMGR YGGEEVNFSS DADLMFVYEA CEGHDEEEAR
TFALRQVDLI RAVLMGVAGT EQKLELDMDL RPEGKNGPLV RSFESYRDYY ARWSETWERQ
ALLRARYAAG DEELGTRFIH DIVDPLRYSE NAVSDAEIQS IRKLKARMEA ERLPRGVRSD
RHIKLGRGGL SDVEWTIQLL QLKHAHEWSD IRTTHTLDAL TALEHHGAMS AKDAAALRDA
WALCTNLRNA SFLWSGRVRQ ADIIPDDFFD MGGLGVVLGH PAHRGAQYLD DVMGIMRKCR
DVVDRLFYGQ EE
//
