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Database: UniProt/TrEMBL
Entry: B1X9D5_ECODH
LinkDB: B1X9D5_ECODH
Original site: B1X9D5_ECODH 
ID   B1X9D5_ECODH            Unreviewed;      1320 AA.
AC   B1X9D5;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   01-MAY-2013, entry version 37.
DE   SubName: Full=Multifunctional proline dehydrogenase, delta-1-pyrroline-5-carboxylate dehydrogenase, and DNA-binding transcriptional regulator;
GN   Name=putA; OrderedLocusNames=ECDH10B_1086;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; CP000948; ACB02215.1; -; Genomic_DNA.
DR   RefSeq; YP_001729993.1; NC_010473.1.
DR   ProteinModelPortal; B1X9D5; -.
DR   SMR; B1X9D5; 2-49, 87-1114.
DR   STRING; 316385.ECDH10B_1086; -.
DR   EnsemblBacteria; ACB02215; ACB02215; ECDH10B_1086.
DR   GeneID; 6059557; -.
DR   KEGG; ecd:ECDH10B_1086; -.
DR   PATRIC; 18462006; VBIEscCol59506_1103.
DR   eggNOG; COG0506; -.
DR   HOGENOM; HOG000253911; -.
DR   KO; K13821; -.
DR   OMA; TGGINAM; -.
DR   ProtClustDB; PRK11809; -.
DR   BioCyc; ECOL316385:GJ8B-1069-MONOMER; -.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:InterPro.
DR   Gene3D; 1.10.2060.10; -; 1.
DR   Gene3D; 1.20.5.550; -; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR025703; Bifunct_PutA.
DR   InterPro; IPR005933; Delta1-pyrroline-5-COlate_DH-3.
DR   InterPro; IPR024090; PRODH_PutA_dom_I.
DR   InterPro; IPR024089; PRODH_PutA_dom_I/II.
DR   InterPro; IPR024082; PRODH_PutA_dom_II.
DR   InterPro; IPR002872; Proline_DH.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   SUPFAM; SSF81935; SSF81935; 1.
DR   TIGRFAMs; TIGR01238; D1pyr5carbox3; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA-binding; Oxidoreductase.
SQ   SEQUENCE   1320 AA;  143815 MW;  E4920143D536F7F9 CRC64;
     MGTTTMGVKL DDATRERIKS AATRIDRTPH WLIKQAIFSY LEQLENSDTL PELPALLSGA
     ANESDEAPTP AEEPHQPFLD FAEQILPQSV SRAAITAAYR RPETEAVSML LEQARLPQPV
     AEQAHKLAYQ LADKLRNQKN ASGRAGMVQG LLQEFSLSSQ EGVALMCLAE ALLRIPDKAT
     RDALIRDKIS NGNWQSHIGR SPSLFVNAAT WGLLFTGKLV STHNEASLSR SLNRIIGKSG
     EPLIRKGVDM AMRLMGEQFV TGETIAEALA NARKLEEKGF RYSYDMLGEA ALTAADAQAY
     MVSYQQAIHA IGKASNGRGI YEGPGISIKL SALHPRYSRA QYDRVMEELY PRLKSLTLLA
     RQYDIGINID AEESDRLEIS LDLLEKLCFE PELAGWNGIG FVIQAYQKRC PLVIDYLIDL
     ATRSRRRLMI RLVKGAYWDS EIKRAQMDGL EGYPVYTRKV YTDVSYLACA KKLLAVPNLI
     YPQFATHNAH TLAAIYQLAG QNYYPGQYEF QCLHGMGEPL YEQVTGKVAD GKLNRPCRIY
     APVGTHETLL AYLVRRLLEN GANTSFVNRI ADTSLPLDEL VADPVTAVEK LAQQEGQTGL
     PHPKIPLPRD LYGHGRDNSA GLDLANEHRL ASLSSALLNS ALQKWQALPM LEQPVAAGEM
     SPVINPAEPK DIVGYVREAT PREVEQALES AVNNAPIWFA TPPAERAAIL HRAAVLMESQ
     MQQLIGILVR EAGKTFSNAI AEVREAVDFL HYYAGQVRDD FANETHRPLG PVVCISPWNF
     PLAIFTGQIA AALAAGNSVL AKPAEQTPLI AAQGIAILLE AGVPPGVVQL LPGRGETVGA
     QLTGDDRVRG VMFTGSTEVA TLLQRNIASR LDAQGRPIPL IAETGGMNAM IVDSSALTEQ
     VVVDVLASAF DSAGQRCSAL RVLCLQDEIA DHTLKMLRGA MAECRMGNPG RLTTDIGPVI
     DSEAKANIER HIQTMRSKGR PVFQAVRENS EDAREWQSGT FVAPTLIELD DFAELQKEVF
     GPVLHVVRYN RNQLPELIEQ INASGYGLTL GVHTRIDETI AQVTGSAHVG NLYVNRNMVG
     AVVGVQPFGG EGLSGTGPKA GGPLYLYRLL ANRPESALAV TLARQDAKYP VDAQLKAALT
     QPLNALREWA ANRPELQALC TQYGELAQAG TQRLLPGPTG ERNTWTLLPR ERVLCIADDE
     QDALTQLAAV LAVGSQVLWP DDALHRQLVK ALPSAVSERI QLAKAENITA QPFDAVIFHG
     DSDQLRALCE AVAARDGTIV SVQGFARGES NILLERLYIE RSLSVNTAAA GGNASLMTIG
//
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