ID D2R6H7_PIRSD Unreviewed; 1032 AA.
AC D2R6H7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
DE Flags: Precursor;
GN OrderedLocusNames=Psta_0870 {ECO:0000313|EMBL:ADB15555.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15555.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB15555.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
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 -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP001848; ADB15555.1; -; Genomic_DNA.
DR AlphaFoldDB; D2R6H7; -.
DR STRING; 530564.Psta_0870; -.
DR KEGG; psl:Psta_0870; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005682_2_0_0; -.
DR OrthoDB; 4503395at2; -.
DR Proteomes; UP000001887; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:InterPro.
DR CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR Gene3D; 3.20.20.220; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
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; IPR002872; Proline_DH_dom.
DR InterPro; IPR041514; PutA_N.
DR InterPro; IPR005932; RocA.
DR NCBIfam; TIGR01237; D1pyr5carbox2; 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; PF18083; PutA_N; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 42..154
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 164..468
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 555..1015
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 792
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 826
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1032 AA; 113140 MW; CDC1A33852FE9305 CRC64;
MITVPSTTLA TSSASASQSA IDALVGPLAA LDVSADTLAT IEARTQAIGR ELFAGLGDVR
PKFWQRRWWD EKLMSWSMSD EQLKVQLFRF VDVLPMLTTA DSVTTHLAEY LEPVQDRLPQ
AARVALGMAR RMPPLRAAVA KAARLSAMDF ARRFIAGETA EQVLRTAEQE RTLGRSFTLD
ILGEAVTSEV EANRYFEAYL KLLGDTSKVA AAWEAHPRVD NDDRGPTPRV NLSVKLSALD
CRFDPIDPEG TFRRAGDKLR TIFHEARRLG AFINVDMESY AKKDLTLDIF QRLLMEPELR
DWTDCGIVLQ CYLRDTPRDV VELRNWAAQR GTPVWVRLVK GAYWDYETLH ARANHWPIPV
YQEKWQSDAV YESVTRFVLQ NRQFLRPALG SHNLRSIAHG IAATEVLGID PAGLEMQMLY
GMADAEKQAL VDRGHRLRIY MPYGELIPGM AYLVRRLLEN TANTSFLRAG FIEHKPIESL
LARPTSHLKL VGASAASTSP DKEKRPMSAT FANQPPVDFA DSHQRAAMLD ALTSVREKLG
RHFPLVIGGR KLDTQERITS TDPSLRTRIV GTTASASAEQ AREAVAAAVQ AMDAWHTSGA
ESRAKVLRKA AEIMRSRLME LSAIEVYECG KTWREATADV DEAIDFLEFY ATGAIKLQRT
RGADVPGEEN RFEYLPRGVT AVIAPWNFPL AILCGMTSAA IAVGNTVVMK PAEQSSIIAG
VFMEILEQAG LPAGVVNFLP GLGEVAGAAL VEHPDVAAII FTGSREVGLA INARAAETSR
KSRVGVKRVI AEMGGKNAII VDSDADLDEA VAGIVHSAFG FQGQKCSACS RAIVLSSVYD
QLLARLVEAT RSLPIGPSEE PSTAIGPVID DESRERIERY IEIGKTEGRT LLATDVSQLV
ERGAFVGPHI FADVSPQARI AQEEIFGPVL AVIRAADLSE AIQIANSTDY ALTGGIFSRS
PHSLERARRE MQVGNLYLNR AITGAMVGRQ PFGGYKMSGI GSKAGGEEYL LQLVVPRTVT
EHTVRRGFAP PE
//
