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Database: UniProt
Entry: A0A0A6CZX7_9SPHN
LinkDB: A0A0A6CZX7_9SPHN
Original site: A0A0A6CZX7_9SPHN 
ID   A0A0A6CZX7_9SPHN        Unreviewed;       436 AA.
AC   A0A0A6CZX7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:KHA64418.1};
DE   Flags: Fragment;
GN   ORFNames=NI18_09210 {ECO:0000313|EMBL:KHA64418.1};
OS   Sphingomonas sp. Ant20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=104605 {ECO:0000313|EMBL:KHA64418.1, ECO:0000313|Proteomes:UP000033201};
RN   [1] {ECO:0000313|EMBL:KHA64418.1, ECO:0000313|Proteomes:UP000033201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant20 {ECO:0000313|EMBL:KHA64418.1,
RC   ECO:0000313|Proteomes:UP000033201};
RA   Ronca S., Frossard A., Guerrero L.D., Makhalanyane T.P., Aislabie J.M.,
RA   Cowan D.A.;
RT   "Draft Genome Sequence of Spingomonas sp. strain Ant20, isolated from oil-
RT   polluted soil near Scott Base, Antarctica.";
RL   Submitted (OCT-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:KHA64418.1}.
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DR   EMBL; JRVI01000054; KHA64418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6CZX7; -.
DR   Proteomes; UP000033201; 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   GO; GO:0016874; F:ligase activity; 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; 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; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:KHA64418.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:KHA64418.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033201};
KW   Transferase {ECO:0000313|EMBL:KHA64418.1}.
FT   DOMAIN          47..226
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          252..383
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   NON_TER         436
FT                   /evidence="ECO:0000313|EMBL:KHA64418.1"
SQ   SEQUENCE   436 AA;  47584 MW;  E65AF51F1ADA0F47 CRC64;
     MIAATQRARR WSPFLAMLLD REPVLARELA EGRLDPIPVP LDPDMPVARR LRLERRALAL
     RVAIGDLAGV FDLTAVTQQL TGFADHALDT AIRTAIEERT PGAEARGFAA IALGKQGSGE
     LNYSSDIDPI LIYDPDTLPL RPREEPEAAA VRIGKRVVEL LQARDGDGYV LRVDLRLRPS
     PEITPIALPI DAAISYYEAQ ALPWERAAFI RARAAAGDIA LVRQFLDTVR PFVWRRALDF
     GAIGEIRGIS RRIRDHHAQG QAFGPGYDLK RGRGGIREAE FFAQIHQLIH GGRDPALRAP
     ATRVALARLA EAGWIGGDEA RALIESYTLL RTIEHRVQMI DDRQTHALPT GDALERVAWL
     HGLDGSAALL ALLAPHVAAT GRIYDALDDG AASGLSHDPT RLDAELAEAG FAEPEPARQR
     IAAWRAGAYP ALRSSA
//
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