ID A0A1Z4RNX4_9CHRO Unreviewed; 991 AA.
AC A0A1Z4RNX4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN Name=putA {ECO:0000313|EMBL:BAZ44153.1};
GN ORFNames=NIES4102_11590 {ECO:0000313|EMBL:BAZ44153.1};
OS Chondrocystis sp. NIES-4102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Chondrocystis.
OX NCBI_TaxID=2005460 {ECO:0000313|EMBL:BAZ44153.1, ECO:0000313|Proteomes:UP000217698};
RN [1] {ECO:0000313|EMBL:BAZ44153.1, ECO:0000313|Proteomes:UP000217698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4102 {ECO:0000313|EMBL:BAZ44153.1,
RC ECO:0000313|Proteomes:UP000217698};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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; AP018281; BAZ44153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4RNX4; -.
DR KEGG; chon:NIES4102_11590; -.
DR OrthoDB; 548310at2; -.
DR Proteomes; UP000217698; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000217698}.
FT DOMAIN 10..125
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 134..440
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 516..974
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 459..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..187
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 751
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 785
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 991 AA; 110454 MW; 51431E4AB6068390 CRC64;
MNLGANLRYE SKTQAIAQEL IKSTREGNNI FSRMRDQMRW DDKVLDWTMA NPGLRVQMFR
FIDTIPALQS KAEIANHFQQ YMSAEAVELP GALKGILNFS DPDSFPAQTA AATITKAVET
LAYKYIAGEN IASVMKTIAR LRKEGMTYTI DLLGEAVITE TEAEEYLKRY LDLIEQLTQQ
AKGWQRVEGI DLASGELLPQ VQVSVKLTAF YSQFDPLDPV GSKAKVCDRL RILLRQAEVL
GAAIHFDMEQ YRYKDLTLQI LKELLMEEEF RTRSDLGITL QAYLRDSYQD LQEIISWVKE
RGYPLTVRLV KGAYWDQETI KSEQNHWQQP VYNQKAATDV NYERMTQLLL ENHQYLYAAI
GSHNVRSQAL ACAIAETLNI PPRRFEMQVL YGMGDKLAQA LVKRGHRVRV YSPYGKLLPG
MAYLIRRLLE NTANSSFLRQ NQENKPVAEL IAPPVVKEED NHRQVNQKNT FQNAPDTDYA
DTAKRQKAQQ TLEEVRQKLG KTYLPLINGE YLETSDYLDS INPARNSELI GKIGQISLEQ
AEMAINAAKE AFKSWKLTPA KTRADILRKA ADLMEQRRHE LNAWICLEVG KIIPQADGEV
SEAIDFCRYY ASEMERLARG INYDLAGENN RYFYQPKGIA VVISPWNFPF AIATGMTVAA
LVTGNCTLLK PAATSSVIAA KLTEILIEAG IPKGVFQYVP GKGSQIGTYL VEHKDTQMIA
FTGSREVGCQ IYAAAAKLQP GQKHLKRVIA EMGGKNAIIV DESADLDQAV VGVVQSAFGY
SGQKCSACSR VIVLAPVYES FLARLIAATQ SLNVGVADDP GMQMSAVIDA PARDRILEYI
EQGKQQSKLV LEMSVPEGGY YISPTIFSQV QPDHVIAQSE IFGPVLAVIQ ADNFDQALTI
ANGTDYALTG GLYSRTPKNI EQAEVEFEVG NLYINRNITG AIVARQPFGG FKLSGVGSKA
GGADYLLQFL DPRVVTENIQ RQGFAPIEGA E
//
