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Database: UniProt
Entry: Q2GK50_ANAPZ
LinkDB: Q2GK50_ANAPZ
Original site: Q2GK50_ANAPZ 
ID   Q2GK50_ANAPZ            Unreviewed;      1045 AA.
AC   Q2GK50;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197};
DE   Includes:
DE     RecName: Full=Proline dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              EC=1.5.5.2 {ECO:0000256|PIRNR:PIRNR000197};
DE     AltName: Full=Proline oxidase {ECO:0000256|PIRNR:PIRNR000197};
DE   Includes:
DE     RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              Short=P5C dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              EC=1.2.1.88 {ECO:0000256|PIRNR:PIRNR000197};
DE     AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
GN   Name=putA {ECO:0000313|EMBL:ABD43975.1};
GN   OrderedLocusNames=APH_0669 {ECO:0000313|EMBL:ABD43975.1};
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD43975.1, ECO:0000313|Proteomes:UP000001943};
RN   [1] {ECO:0000313|EMBL:ABD43975.1, ECO:0000313|Proteomes:UP000001943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZ {ECO:0000313|EMBL:ABD43975.1,
RC   ECO:0000313|Proteomes:UP000001943};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC       nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC         glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC         Evidence={ECO:0000256|ARBA:ARBA00001468,
CC         ECO:0000256|PIRNR:PIRNR000197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC         quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:132124; EC=1.5.5.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC       {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004786, ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the proline
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
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DR   EMBL; CP000235; ABD43975.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2GK50; -.
DR   STRING; 212042.APH_0669; -.
DR   PaxDb; 212042-APH_0669; -.
DR   EnsemblBacteria; ABD43975; ABD43975; APH_0669.
DR   KEGG; aph:APH_0669; -.
DR   eggNOG; COG0506; Bacteria.
DR   eggNOG; COG4230; Bacteria.
DR   HOGENOM; CLU_005682_1_0_5; -.
DR   OMA; PPWNFPV; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000001943; Chromosome.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR   CDD; cd07125; ALDH_PutA-P5CDH; 1.
DR   Gene3D; 3.20.20.220; -; 1.
DR   Gene3D; 1.20.5.460; Single helix bin; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR025703; Bifunct_PutA.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR041349; PRODH.
DR   InterPro; IPR024089; PRODH_PutA_dom_I/II.
DR   InterPro; IPR024082; PRODH_PutA_dom_II.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR005933; PutA_C.
DR   NCBIfam; TIGR01238; D1pyr5carbox3; 1.
DR   PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   Pfam; PF14850; Pro_dh-DNA_bdg; 1.
DR   Pfam; PF18327; PRODH; 1.
DR   PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR   SUPFAM; SSF81935; N-terminal domain of bifunctional PutA protein; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR000197};
KW   FAD {ECO:0000256|PIRNR:PIRNR000197};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000197};
KW   NAD {ECO:0000256|PIRNR:PIRNR000197};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000197};
KW   Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN          11..57
FT                   /note="Proline utilization A proline dehydrogenase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18327"
FT   DOMAIN          65..176
FT                   /note="Proline dehydrogenase PutA"
FT                   /evidence="ECO:0000259|Pfam:PF14850"
FT   DOMAIN          186..479
FT                   /note="Proline dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
FT   DOMAIN          575..1026
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        798
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT   ACT_SITE        832
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ   SEQUENCE   1045 AA;  114580 MW;  52DECF460A25D883 CRC64;
     MMISSLQVPD ELRKRMQGLY NTDEKSYIRY LTEKAEVSQD AKVRIYNLAK QIIEKVRFGK
     GSTLIDAFMQ EYGLSSEEGV ALMCLAESLL RIPDECTIDE MIRDKIAGTT WKKHIGSSSS
     IFVNASTLAL CVGARVLREV DDSRWYSVLS NLLKNMGEPI IRKAALQAMC ILGKHFVMGR
     DIEDAVARSN DSKQLCSFDI LGESARTRED ADRYFAAYMH AIEVIGADAG CGDDISSRHG
     ISVKLSALHP RYDFAQIDYV LDDISSKLLE ICAAAKKHNI GVLIDAEEAR RLEASLIVLE
     KVFLDKSLDG WEGLGLAVQA YQKRALGVLD IVEDIAIRAN RKMVVRLVKG AYWDYEIKNA
     QELGLDGYPV FTRRAYTDTS YFACVQRILS KPNTFYPCFA THNAYTLASV LESADKDHPG
     FEFQRLHAMG QGLYSYVTGE VAPSVKCRVY APVGSYQDLL PYLIRRLLEN GTNSSFVNKI
     NDVDVLAEQL LVDPLEKAKS FEYCPHPSIP LPIDMFGKDR VNSIGLNTSD SLAMSVLNEE
     VQTFTNVTRK ATPIINGEDV EGAAPIEFFS PGDFSCKVGE VSYATPEQVK EAFAVAHAAY
     AEWSALSVEE RATILESAAD LLEKERGKFV ALLMLEGGKV ISDVMAEIRE AVDFLRYYAM
     IARKDIAGTI KLPGPSGEEN YIYFESRGVF VCISPWNFPL AIFLGPIAAA LVTGNTVIAK
     PSEQTSLIAY EAVKLFFRAG LPGSVLQFLP GEGAALGEVL INNGHVAGVA FTGSTDTANI
     INRTLAKRNR DIVPIIAETG GINAMIVDSS AVLEQVCDDV ITSAFRSAGQ RCSALRVLLL
     QEEIADRQIE IICGALKELR LGNPMLLSSD VGPVIDQQSY DMLCEYVKGM EEKGAKLLCK
     LDIGSLAEVG HYFPPHIFEV GSVSEVAKEV FGPILHIVRY KKSDLVSILE EINKTGYGLT
     FSVQSRIQSN IDLIVDKIRT GNVYVNRNQI GAVVGVQPFG GSGLSGTGPK AGGPFYLHRF
     VTEKTVTVNT TALGGNVALA CLEEE
//
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