GSA_SYNP6
ID GSA_SYNP6 Reviewed; 433 AA.
AC P24630; Q5N3P9;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase;
DE Short=GSA;
DE EC=5.4.3.8;
DE AltName: Full=Glutamate-1-semialdehyde aminotransferase;
DE Short=GSA-AT;
GN Name=hemL; Synonyms=gsa; OrderedLocusNames=syc0881_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1900346; DOI=10.1007/bf00282635;
RA Grimm B., Bull A., Breu V.;
RT "Structural genes of glutamate 1-semialdehyde aminotransferase for
RT porphyrin synthesis in a cyanobacterium and Escherichia coli.";
RL Mol. Gen. Genet. 225:1-10(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1905724; DOI=10.1016/s0021-9258(18)98926-x;
RA Grimm B., Smith A.J., Kannangara C.G., Smith M.;
RT "Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of
RT Synechococcus. Deletion of a tripeptide close to the NH2 terminus and
RT internal amino acid substitution.";
RL J. Biol. Chem. 266:12495-12501(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-17.
RX PubMed=2505791; DOI=10.1007/bf02907586;
RA Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.;
RT "Purification and partial amino acid sequence of the glutamate 1-
RT semialdehyde aminotransferase of barley and synechococcus.";
RL Carlsberg Res. Commun. 54:67-79(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9144156; DOI=10.1073/pnas.94.10.4866;
RA Hennig M., Grimm B., Contestabile R., John R.A., Jansonius J.N.;
RT "Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-
RT dimeric vitamin B6-dependent enzyme with asymmetry in structure and active
RT site reactivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4866-4871(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC EC=5.4.3.8;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. HemL subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD79071.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X53695; CAA37733.1; -; Genomic_DNA.
DR EMBL; AP008231; BAD79071.1; ALT_INIT; Genomic_DNA.
DR PIR; S13326; S13326.
DR RefSeq; WP_011243193.1; NC_006576.1.
DR PDB; 2GSA; X-ray; 2.40 A; A/B=2-433.
DR PDB; 2HOY; X-ray; 2.20 A; A/B=2-433.
DR PDB; 2HOZ; X-ray; 2.20 A; A/B=2-433.
DR PDB; 2HP1; X-ray; 2.08 A; A/B=2-433.
DR PDB; 2HP2; X-ray; 2.70 A; A/B=2-433.
DR PDB; 3FQ7; X-ray; 2.15 A; A/B=7-433.
DR PDB; 3FQ8; X-ray; 2.00 A; A/B=7-433.
DR PDB; 3FQA; X-ray; 2.35 A; A/B=7-433.
DR PDB; 3GSB; X-ray; 3.00 A; A/B=2-433.
DR PDB; 4GSA; X-ray; 2.50 A; A/B=2-433.
DR PDBsum; 2GSA; -.
DR PDBsum; 2HOY; -.
DR PDBsum; 2HOZ; -.
DR PDBsum; 2HP1; -.
DR PDBsum; 2HP2; -.
DR PDBsum; 3FQ7; -.
DR PDBsum; 3FQ8; -.
DR PDBsum; 3FQA; -.
DR PDBsum; 3GSB; -.
DR PDBsum; 4GSA; -.
DR AlphaFoldDB; P24630; -.
DR SMR; P24630; -.
DR DIP; DIP-61261N; -.
DR STRING; 269084.syc0881_c; -.
DR DrugBank; DB02054; Gabaculine.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR EnsemblBacteria; BAD79071; BAD79071; syc0881_c.
DR KEGG; syc:syc0881_c; -.
DR eggNOG; COG0001; Bacteria.
DR BRENDA; 5.4.3.8; 6187.
DR UniPathway; UPA00251; UER00317.
DR UniPathway; UPA00668; -.
DR EvolutionaryTrace; P24630; -.
DR Proteomes; UP000001175; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00713; hemL; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chlorophyll biosynthesis; Cytoplasm;
KW Direct protein sequencing; Isomerase; Porphyrin biosynthesis;
KW Pyridoxal phosphate.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..433
FT /note="Glutamate-1-semialdehyde 2,1-aminomutase"
FT /id="PRO_0000120461"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 51
FT /note="Y -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="I -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..134
FT /note="LM -> VV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="D -> S (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="S -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="A -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:3FQ7"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2HOZ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2GSA"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 247..252
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:3GSB"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3FQ8"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 328..349
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:3FQ8"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:3FQ8"
FT HELIX 416..432
FT /evidence="ECO:0007829|PDB:3FQ8"
SQ SEQUENCE 433 AA; 46116 MW; 83585133A666B923 CRC64;
MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA YAWDVDGNRY
IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE NVLAEMVIDA VPSIEMVRFV
NSGTEACMAV LRLMRAYTGR DKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPKST
TANTLTAPYN DLEAVKALFA ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA
LLVFDEVMTG FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM
YQAGTLSGNP LAMTAGIKTL ELLRQPATYE YLDQITKRLS DGLLAIAQET GHAACGGQVS
GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL APSQFEAGFT SLAHTEEDID
ATLAAARTVM SAL
