ID A0A220VD87_9GAMM Unreviewed; 744 AA.
AC A0A220VD87;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:ASK78309.1};
GN ORFNames=CF386_04405 {ECO:0000313|EMBL:ASK78309.1};
OS Paraphotobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Paraphotobacterium.
OX NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK78309.1, ECO:0000313|Proteomes:UP000242175};
RN [1] {ECO:0000313|EMBL:ASK78309.1, ECO:0000313|Proteomes:UP000242175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK78309.1,
RC ECO:0000313|Proteomes:UP000242175};
RX PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA Huang Z., Dong C., Shao Z.;
RT "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT Vibrionaceae, isolated from surface seawater.";
RL Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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DR EMBL; CP022355; ASK78309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220VD87; -.
DR KEGG; pmai:CF386_04405; -.
DR Proteomes; UP000242175; Chromosome large.
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; 1.
DR Gene3D; 1.20.120.1510; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
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; 1.
DR Pfam; PF03710; GlnE; 2.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
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:ASK78309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242175};
KW Transferase {ECO:0000313|EMBL:ASK78309.1}.
FT DOMAIN 65..304
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 344..467
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 583..737
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
SQ SEQUENCE 744 AA; 87039 MW; C835FB782E05E09E CRC64;
MRLFVILFSN VRSKCNQRLI LNWSNDLSNT CCSLSKDYIK KYLNSEFCQN KKTHESVVNY
IYYSANKSKF IHDSLKQKPS LIRDLFLKLK NRDHLNNYKK LNIKNHINNS INDEKRYFQE
LRYFHKLETL TIAVLDLNDL ETIQQIVKRQ SKLAEQLVLV AYAWCYSTLK KSLGTPLDKL
NQELHMKILA MGKLGGDELN FSSDIDLIFC FPFEGITVGG KKSISHSEFF TRVGQKLISC
LNQSTSDGYC YRVDMRLRPY GDSGALVYSF SALEEYYQSQ GREWERYALV KAKILGENDS
FSQKLRLKLL PFVFRKYIDF SIIDSLKLMK KKINIESKHV NNNILNIKLG CGGIREAEFI
VQSFQLVRGG REEGLRSRNF NEALIAINKL KLLSDKETQN LKKSYWFLRQ LENYLQILDN
KQVHHLPNNE KEQRIIQKLF KFDFWENFLE TLAFHTHNIH KIFQHIFGNE EDTNDSNNVF
QNIWLLSDKK DVLNKLLLDL NQNEPNQITS IISNFKKSLR KKNIGKFGKI NLDLLIPKSL
QIILNLQISN KSDVLKRMFD ILFNIVTRTT YLELLNKYNF VLEELINLVS KSTFVTQQIT
KYPILLDEIL TTDGKLTLLN LEDYKGELEN LSLSFHQDDF EQQMELLRQF KQSQIFKIVV
SDLRNKIPLM KVSDHLTALA ESIIHKVTEL AWHQITNQYG IPSYLEGSSF KDFTIIGFGK
LGGYELSYNS DLDLVFCQIF QKHL
//
