ID   Y929_HAEIN              Reviewed;         393 AA.
AC   P44940;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative acid--amine ligase HI_0929;
DE            EC=6.3.1.-;
GN   OrderedLocusNames=HI_0929;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: May be a ligase forming an amide bond. Shows ATPase activity
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutathionylspermidine synthase preATP-grasp
CC       family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22589.1; -; Genomic_DNA.
DR   PIR; F64161; F64161.
DR   RefSeq; NP_439089.1; NC_000907.1.
DR   RefSeq; WP_010869087.1; NC_000907.1.
DR   AlphaFoldDB; P44940; -.
DR   SMR; P44940; -.
DR   STRING; 71421.HI_0929; -.
DR   PRIDE; P44940; -.
DR   EnsemblBacteria; AAC22589; AAC22589; HI_0929.
DR   KEGG; hin:HI_0929; -.
DR   PATRIC; fig|71421.8.peg.970; -.
DR   eggNOG; COG0754; Bacteria.
DR   HOGENOM; CLU_059175_0_0_6; -.
DR   OMA; QWNSLHE; -.
DR   PhylomeDB; P44940; -.
DR   BioCyc; HINF71421:G1GJ1-969-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR005494; GSPS_pre-ATP-grasp-like_dom.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF03738; GSP_synth; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..393
FT                   /note="Putative acid--amine ligase HI_0929"
FT                   /id="PRO_0000169404"
FT   BINDING         103..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         378..380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            103
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  45792 MW;  D2773A5BF35E8B38 CRC64;
     MKRVTGFPTR PDMVQQLLNV GFDYYNLPSS DGSHYWSDNV AYEFTLAEID RIEDTTNELH
     SMCLDFAADE IKKGDYENYH FTELQKQLIE TSWRNQEPYL YGRFDFGYDG NNLKMFEYNA
     DTPTSLLEAA VVQWQWLEQI EGLKHRDQFN WIHEELIKHF QFLKQQSGKT DFHLSAMQDA
     GREDWGNVDY LADVAYNAGW NIHQLAVEDI GYNSETKKFV DLNDQPIEML FKLYPLEWLS
     HAEFARHITT AETRFIEPAW KMLLSNKALL AKLWARYPNH PHLLPAYFTP FELPKDLSMW
     VKKPLLGREG ANVFYYEKNN GVEFAAKGSE HSTFYGNSGY VYQQKFELPS FDGMYPIIGS
     WVVGDVACGM GLREDFTAVT GNDSHFIPHY FVP