ID A0A077MFF3_9MICO Unreviewed; 1080 AA.
AC A0A077MFF3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=BN13_510012 {ECO:0000313|EMBL:CCI53942.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI53942.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI53942.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53942.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI53942.1}.
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DR EMBL; CAJC01000163; CCI53942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077MFF3; -.
DR STRING; 1193518.BN13_510012; -.
DR Proteomes; UP000035720; Unassembled WGS sequence.
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 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 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 PIRSF; PIRSF000197; Bifunct_PutA; 2.
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:UP000035720}.
FT DOMAIN 137..429
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 508..921
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 699
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 733
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1080 AA; 115588 MW; D4AF028FCD0CABD5 CRC64;
MPKVTDPRDE ARVEAAIALA GRLLSTATAD ITPAERRRQD RLAGLIEDVE GRELVQALTD
EVLRIDRPKR AANRFRRIVA EHGVPRSLGL IDRGLMALGA RLAPGLPPLV MPLATRRIVA
ETHGLVIPAE DPALGAHIAA RRAAGVDLNI NVLGEAILSD AEADARLARV QATMARRDVT
YVSVKISALC AQLDVAAFDH SVDRICDRLE VIFRAALAAR PPVFVNLDME EYADLHLTVA
AFTRVLSQEE FRTAPAGIVL QAYLPDSHAV LDHLATWSAA RVAAGGPPIK IRIVKGANLA
MERVDAEQHG WVQAPYPLKS DVDASYKRLL DAALGHVATG TLRLGVASHN LFDIAWALTL
IGELPAARRA GVEIEMLEGM VPAQARAVLA EAGSLLFYCP IVRDDEIEAS LAYLARRFDE
NTGRDNFLRA MFTMEPGSAS FEEQAGRFRA AVAARHTVST TPRRPGLAET GDGFHNAPDS
DFTAALVRGQ LAAAMAQLPD VTVDVVTTPA DVDEVVARIV AGQAAWAART SAERAALLNT
VADRMEADRF ATLALMADEA GKTAREGDPE VSEGIDFARY YATADLPAES EPIGSVLIAS
PWNFPYAIPA GGVFAALMAG NTVVLKPAPE TRRIAKWLVD QCHAAGIPQD ALQYLACPDD
DTGRHLITHD AFGTLILTGS YDSAKLFLGW KPRLRVLAET SGKNALVVTE AADQDAAIKD
IVKSAFGHAG QKCSAASLAI VEAPVYDDPD FRRRLADAVA TVRVGWGPDP ATIMGPLISP
PGEALERGLT RLDAGESWLV EPRQLDDSGR LWSPGVRIGV QPGSWFHRTE CFGPVLGVVR
AHDLADAIAI QNGTAYGLTA GLHSLDPGEI DTWLAAVEAG NLYVNRHITG AIVRRQPFGG
WKRSAIGGGP KAGGPDYVAA FRRHPSVAID FAAAAAAYRT AWDQRFGVES DPSALVSEAN
IHRYRPLGAV MVRFGADTPD GAVDAARAAS AVCRTGRLAV FGPESDDAAL VRALRSDRPD
RLRLLTEAGE DVLRVCHELD IAVVTQPVSA DAAAELPLWL HEQALSISRH RYGRVAGVEI
//
