ID A0A261EVN9_9BIFI Unreviewed; 1063 AA.
AC A0A261EVN9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamine-synthetase adenylyltransferase {ECO:0000313|EMBL:OZG50931.1};
GN ORFNames=BOCO_0117 {ECO:0000313|EMBL:OZG50931.1};
OS Bombiscardovia coagulans.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bombiscardovia.
OX NCBI_TaxID=686666 {ECO:0000313|EMBL:OZG50931.1, ECO:0000313|Proteomes:UP000216004};
RN [1] {ECO:0000313|EMBL:OZG50931.1, ECO:0000313|Proteomes:UP000216004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22924 {ECO:0000313|EMBL:OZG50931.1,
RC ECO:0000313|Proteomes:UP000216004};
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:OZG50931.1}.
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DR EMBL; MWWS01000002; OZG50931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261EVN9; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000216004; 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:OZG50931.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216004};
KW Transferase {ECO:0000313|EMBL:OZG50931.1}.
FT DOMAIN 119..368
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 389..487
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 652..893
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 917..1059
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 119170 MW; EB850223B370FE06 CRC64;
MKADDKSFGL ALSSVDLIRA GLRDLGKARQ ELSELSAKGL GQAGGKVLLT ALSQTCEPDR
ALESLVRIIE SSEDWSPQRT STLSNGGGNK DTSATSLNKP SAWARCSLNW LSQHPQSLTQ
LVNVLGASQA MGILMQNRPR LVAAVTTAVT DLKNSTVTNE DDIVAVVSAH CQHGSNFDYA
SAVNDLREAY YRRLAVIMVK DLSSDDAERD QPLISSQLSQ LADECLQAAL MIAKRRVAQS
HECKFVIIGM GKLGARELNY VSDVDLVYAV EPVHPGGVVS SEQLIQIGSK IAVTLQQVCQ
SAITGVCEPP LWKVDTALRP EGKHGPLVRT LASYREYYDS WAENWEFQAL IKARALAGDM
ELGREFENMC DEFVWSAAQR PNFVYDCQQM RKRVERLIPS KLKDREIKLG QGGLRDVEFT
VQMLQMVHGR TDLSLRTRST LEALNALASA GYVSSRHAER LAADYRFERV LEHRQQMWLL
KRTHLFPDLG THNRGGLDFR RNLTIEDLDG NEDIYRLSRA FHIHPDELVE RYDQTRREIR
TLHLTIFFRP MLPIDAQLDD GEMSLEPHAA KERFASIGFA DPEAAFRHVQ ALTRGLTRSA
KINRILLPAV IAWLGNGQDP DMGLLGWRTL EERFGNKSAY LGFLRDSTSA AKRLCHVLSN
SRYLGSALCK SVESVTWLGD DQLLHPRTLE SLTVSCDSFR QRHADSIGDF ANALRSMRRR
EIERIGLGWM NHVCSEDACL RGMSDVYDAM LQAALQWSRA NQVTQMSVDD EPARIAIIAL
GRYGGQEVNF SSDADIMIVY EPNEGVSDQQ AAHYAQAVCN QLRSIVMSMT LSVEPKLDID
LDLRPEGRSG PIVRSFKSCK HYYQQWSSVW EHQALLRARY AAGDTQLCER FLQEIANPIR
YPMTSLQDMQ IAEIRKLKAR MEAERLPRGV RRDRHLKLGA GGLSDVEWTV QLLQLEHAGR
HPELQVTSTK GALRALSSLR LIDIEDANAL EHGWQMCTSA RNGNYLWLGK INQADILPDD
TYTLGAMAVY SGYPAHRGAE FANELLAAMR RSREVVSRLF YGE
//
