Q7M523 (1A1D_CYBSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: 1-aminocyclopropane-1-carboxylate deaminase Short name=ACC deaminase Short name=ACCD EC=3.5.99.7
Organism	Cyberlindnera saturnus (Yeast) (Williopsis saturnus)
Taxonomic identifier	907340 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Phaffomycetaceae › Cyberlindnera

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate.
Catalytic activity	1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3.
Cofactor	Pyridoxal phosphate.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the ACC deaminase/D-cysteine desulfhydrase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	amine catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	1-aminocyclopropane-1-carboxylate deaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 341

341

1-aminocyclopropane-1-carboxylate deaminase

PRO_0000184512

Sites

Active site

78

1

Nucleophile

Amino acid modifications

Modified residue

1

1

N-acetylserine Ref.1

Modified residue

51

1

N6-(pyridoxal phosphate)lysine

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

341

Helix Strand Turn

Details...

Turn

2 – 4

3

Beta strand

12 – 15

4

Beta strand

18 – 20

3

Helix

22 – 27

6

Turn

28 – 30

3

Beta strand

32 – 38

7

Helix

39 – 41

3

Helix

50 – 55

6

Turn

56 – 58

3

Helix

59 – 64

6

Beta strand

68 – 75

8

Helix

79 – 91

13

Beta strand

94 – 100

7

Helix

107 – 109

3

Turn

110 – 115

6

Helix

117 – 124

8

Beta strand

128 – 131

4

Helix

142 – 153

12

Beta strand

158 – 161

4

Helix

163 – 165

3

Turn

169 – 173

5

Helix

174 – 189

16

Beta strand

194 – 203

10

Helix

204 – 213

10

Helix

214 – 216

3

Helix

219 – 221

3

Beta strand

222 – 226

5

Helix

231 – 249

19

Helix

274 – 287

14

Turn

293 – 295

3

Helix

296 – 308

13

Beta strand

317 – 322

6

Helix

326 – 335

10

Sequences

	Sequence		Length	Mass (Da)
	Q7M523 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 64904CDD7AA2C5FA	FASTA	341	37,061
	10 20 30 40 50 60 SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN KLRKLEYIVP 70 80 90 100 110 120 DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE DWVPIPEAEK DVYNRVGNIE 130 140 150 160 170 180 LSRIMGADVR VIEDGFDIGM RKSFANALQE LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD 190 200 210 220 230 240 EVINQEVELG IKFDKIVVCC VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR 250 260 270 280 290 300 IANNTAKLIG VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM 310 320 330 340 QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A

References

[1]	"Properties, sequence, and synthesis in Escherichia coli of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus." Minami R., Uchiyama K., Murakami T., Kawai J., Mikami K., Yamada T., Yokoi D., Ito H., Matsui H., Honma M. J. Biochem. 123:1112-1118(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, CHARACTERIZATION, ACETYLATION AT SER-1.
[2]	"Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus." Yao M., Ose T., Sugimoto H., Horiuchi A., Nakagawa A., Wakatsuki S., Yokoi D., Murakami T., Honma M., Tanaka I. J. Biol. Chem. 275:34557-34565(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[3]	"Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction." Ose T., Fujino A., Yao M., Watanabe N., Honma M., Tanaka I. J. Biol. Chem. 278:41069-41076(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

Cross-references

Sequence databases

PIR

PW0041.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F2D	X-ray	2.00	A/B/C/D	2-341	[»]
1J0C	X-ray	2.75	A/B/C/D	2-341	[»]
1J0D	X-ray	2.20	A/B/C/D	2-341	[»]
1J0E	X-ray	2.45	A/B/C/D	2-341	[»]

ProteinModelPortal

Q7M523.

SMR

Q7M523. Positions 1-341.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR027278. ACCD_DCysDesulf.
IPR005965. ACP_carboxylate_deaminase.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]

Pfam

PF00291. PALP. 1 hit.
[Graphical view]

PIRSF

PIRSF006278. ACCD_DCysDesulf. 1 hit.

SUPFAM

SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.

TIGRFAMs

TIGR01274. ACC_deam. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q7M523.

Entry information

Entry name

1A1D_CYBSA

Accession

Primary (citable) accession number: Q7M523

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program